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Journal articles on the topic 'Dockerina'

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Published: 4 June 2021
Last updated: 1 February 2022

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1

Pinheiro, Benedita A., Harry J. Gilbert, Kazutaka Sakka, et al. "Functional insights into the role of novel type I cohesin and dockerin domains from Clostridium thermocellum." Biochemical Journal 424, no. 3 (2009): 375–84. http://dx.doi.org/10.1042/bj20091152.

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Cellulosomes, synthesized by anaerobic microorganisms such as Clostridium thermocellum, are remarkably complex nanomachines that efficiently degrade plant cell wall polysaccharides. Cellulosome assembly results from the interaction of type I dockerin domains, present on the catalytic subunits, and the cohesin domains of a large non-catalytic integrating protein that acts as a molecular scaffold. In general, type I dockerins contain two distinct cohesin-binding interfaces that appear to display identical ligand specificities. Inspection of the C. thermocellum genome reveals 72 dockerin-containi
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2

Cameron, Kate, Victor D. Alves, Pedro Bule, Luís M. A. Ferreira, Carlos M. G. A. Fontes, and Shabir Najmudin. "Purification, crystallization and preliminary X-ray characterization of the third ScaB cohesin in complex with an ScaA X-dockerin fromAcetivibrio cellulolyticus." Acta Crystallographica Section F Structural Biology Communications 70, no. 5 (2014): 656–58. http://dx.doi.org/10.1107/s2053230x1400750x.

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Interactions between cohesin and dockerin modules are critical for the formation of the cellulosome, which is responsible for the efficient degradation of plant cell-wall carbohydrates by anaerobes. Type I dockerin modules found in modular enzymatic components interact with type I cohesins in primary scaffoldins, enabling the assembly of the multi-enzyme complex. In contrast, type II dockerins located in primary scaffoldins bind to type II cohesins in adaptor scaffoldins or anchoring scaffoldins located at the bacterial envelope, contributing to the cell-surface attachment of the entire comple
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3

Rincon, Marco T., Tadej Čepeljnik, Jennifer C. Martin, et al. "Unconventional Mode of Attachment of the Ruminococcus flavefaciens Cellulosome to the Cell Surface." Journal of Bacteriology 187, no. 22 (2005): 7569–78. http://dx.doi.org/10.1128/jb.187.22.7569-7578.2005.

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ABSTRACT Sequence extension of the scaffoldin gene cluster from Ruminococcus flavefaciens revealed a new gene (scaE) that encodes a protein with an N-terminal cohesin domain and a C terminus with a typical gram-positive anchoring signal for sortase-mediated attachment to the bacterial cell wall. The recombinant cohesin of ScaE was recovered after expression in Escherichia coli and was shown to bind to the C-terminal domain of the cellulosomal structural protein ScaB, as well as to three unknown polypeptides derived from native cellulose-bound Ruminococcus flavefaciens protein extracts. The Sca
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4

Rincon, Marco T., Shi-You Ding, Sheila I. McCrae, et al. "Novel Organization and Divergent Dockerin Specificities in the Cellulosome System of Ruminococcus flavefaciens." Journal of Bacteriology 185, no. 3 (2003): 703–13. http://dx.doi.org/10.1128/jb.185.3.703-713.2003.

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ABSTRACT The DNA sequence coding for putative cellulosomal scaffolding protein ScaA from the rumen cellulolytic anaerobe Ruminococcus flavefaciens 17 was completed. The mature protein exhibits a calculated molecular mass of 90,198 Da and comprises three cohesin domains, a C-terminal dockerin, and a unique N-terminal X domain of unknown function. A novel feature of ScaA is the absence of an identifiable cellulose-binding module. Nevertheless, native ScaA was detected among proteins that attach to cellulose and appeared as a glycosylated band migrating at around 130 kDa. The ScaA dockerin was pr
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5

Caspi, Jonathan, Yoav Barak, Rachel Haimovitz, et al. "Effect of Linker Length and Dockerin Position on Conversion of a Thermobifida fusca Endoglucanase to the Cellulosomal Mode." Applied and Environmental Microbiology 75, no. 23 (2009): 7335–42. http://dx.doi.org/10.1128/aem.01241-09.

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ABSTRACT We have been developing the cellulases of Thermobifida fusca as a model to explore the conversion from a free cellulase system to the cellulosomal mode. Three of the six T. fusca cellulases (endoglucanase Cel6A and exoglucanases Cel6B and Cel48A) have been converted in previous work by replacing their cellulose-binding modules (CBMs) with a dockerin, and the resultant recombinant “cellulosomized” enzymes were incorporated into chimeric scaffolding proteins that contained cohesin(s) together with a CBM. The activities of the resultant designer cellulosomes were compared with an equival
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6

Park, Jae-Seon, Yutaka Matano, and Roy H. Doi. "Cohesin-Dockerin Interactions of Cellulosomal Subunits of Clostridium cellulovorans." Journal of Bacteriology 183, no. 18 (2001): 5431–35. http://dx.doi.org/10.1128/jb.183.18.5431-5435.2001.

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ABSTRACT The cellulosome of Clostridium cellulovorans consists of three major subunits: CbpA, EngE, and ExgS. The C. cellulovorans scaffolding protein (CbpA) contains nine hydrophobic repeated domains (cohesins) for the binding of enzymatic subunits. Cohesin domains are quite homologous, but there are some questions regarding their binding specificity because some of the domains have regions of low-level sequence similarity. Two cohesins which exhibit 60% sequence similarity were investigated for their ability to bind cellulosomal enzymes. Cohesin 1 (Coh1) was found to contain amino acid resid
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7

Xu, Qi, Edward A. Bayer, Milana Goldman, Rina Kenig, Yuval Shoham, and Raphael Lamed. "Architecture of the Bacteroides cellulosolvens Cellulosome: Description of a Cell Surface-Anchoring Scaffoldin and a Family 48 Cellulase." Journal of Bacteriology 186, no. 4 (2004): 968–77. http://dx.doi.org/10.1128/jb.186.4.968-977.2004.

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ABSTRACT A large gene downstream of the primary Bacteroides cellulosolvens cellulosomal scaffoldin (cipBc, now renamed scaA) was sequenced. The gene, termed scaB, contained an N-terminal leader peptide followed by 10 type I cohesins, an “X” domain of unknown structure and function, and a C-terminal S-layer homology (SLH) surface-anchoring module. In addition, a previously identified gene in a different part of the genome, encoding for a dockerin-borne family 48 cellulosomal glycoside hydrolase (Cel48), was sequenced completely, and a putative cellulosome-related family 9 glycosyl hydrolase was
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8

Jeon, Sang Duck, Ji Eun Lee, Su Jung Kim, Sung Hyun Park, Gi-Wook Choi, and Sung Ok Han. "Unique Contribution of the Cell Wall-Binding Endoglucanase G to the Cellulolytic Complex in Clostridium cellulovorans." Applied and Environmental Microbiology 79, no. 19 (2013): 5942–48. http://dx.doi.org/10.1128/aem.01400-13.

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ABSTRACTThe cellulosomes produced byClostridium cellulovoransare organized by the specific interactions between the cohesins in the scaffolding proteins and the dockerins of the catalytic components. Using a cohesin biomarker, we identified a cellulosomal enzyme which belongs to the glycosyl hydrolase family 5 and has a domain of unknown function 291 (DUF291) with functions similar to those of the surface layer homology domain inC. cellulovorans. The purified endoglucanase G (EngG) had the highest synergistic degree with exoglucanase (ExgS) in the hydrolysis of crystalline cellulose (EngG/ExgS
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9

Krauss, Jan, Vladimir V. Zverlov, and Wolfgang H. Schwarz. "In VitroReconstitution of the Complete Clostridium thermocellum Cellulosome and Synergistic Activity on Crystalline Cellulose." Applied and Environmental Microbiology 78, no. 12 (2012): 4301–7. http://dx.doi.org/10.1128/aem.07959-11.

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ABSTRACTArtificial cellulase complexes active on crystalline cellulose were reconstitutedin vitrofrom a native mix of cellulosomal enzymes and CipA scaffoldin. Enzymes containing dockerin modules for binding to the corresponding cohesin modules were prepared from culture supernatants of aC. thermocellum cipAmutant. They were reassociated to cellulosomes via dockerin-cohesin interaction. Recombinantly produced mini-CipA proteins with one to three cohesins either with or without the carbohydrate-binding module (CBM) and the complete CipA protein were used as the cellulosomal backbone. The bindin
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10

Mingardon, Florence, Ang�lique Chanal, Ana M. L�pez-Contreras, Cyril Dray, Edward A. Bayer, and Henri-Pierre Fierobe. "Incorporation of Fungal Cellulases in Bacterial Minicellulosomes Yields Viable, Synergistically Acting Cellulolytic Complexes." Applied and Environmental Microbiology 73, no. 12 (2007): 3822–32. http://dx.doi.org/10.1128/aem.00398-07.

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ABSTRACT Artificial designer minicellulosomes comprise a chimeric scaffoldin that displays an optional cellulose-binding module (CBM) and bacterial cohesins from divergent species which bind strongly to enzymes engineered to bear complementary dockerins. Incorporation of cellulosomal cellulases from Clostridium cellulolyticum into minicellulosomes leads to artificial complexes with enhanced activity on crystalline cellulose, due to enzyme proximity and substrate targeting induced by the scaffoldin-borne CBM. In the present study, a bacterial dockerin was appended to the family 6 fungal cellula
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11

Xu, Qi, Yoav Barak, Rina Kenig, Yuval Shoham, Edward A. Bayer, and Raphael Lamed. "A Novel Acetivibrio cellulolyticus Anchoring Scaffoldin That Bears Divergent Cohesins." Journal of Bacteriology 186, no. 17 (2004): 5782–89. http://dx.doi.org/10.1128/jb.186.17.5782-5789.2004.

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ABSTRACT Sequencing of a cellulosome-integrating gene cluster in Acetivibrio cellulolyticus was completed. The cluster contains four tandem scaffoldin genes (scaA, scaB, scaC, and scaD) bounded upstream and downstream, respectively, by a presumed cellobiose phosphorylase and a nucleotide methylase. The sequences and properties of scaA, scaB, and scaC were reported previously, and those of scaD are reported here. The scaD gene encodes an 852-residue polypeptide that includes a signal peptide, three cohesins, and a C-terminal S-layer homology (SLH) module. The calculated molecular weight of the
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12

Ding, Shi-You, Edward A. Bayer, David Steiner, Yuval Shoham, and Raphael Lamed. "A Novel Cellulosomal Scaffoldin fromAcetivibrio cellulolyticus That Contains a Family 9 Glycosyl Hydrolase." Journal of Bacteriology 181, no. 21 (1999): 6720–29. http://dx.doi.org/10.1128/jb.181.21.6720-6729.1999.

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ABSTRACT A novel cellulosomal scaffoldin gene, termed cipV, was identified and sequenced from the mesophilic cellulolytic anaerobeAcetivibrio cellulolyticus. Initial identification of the protein was based on a combination of properties, including its high molecular weight, cellulose-binding activity, glycoprotein nature, and immuno-cross-reactivity with the cellulosomal scaffoldin ofClostridium thermocellum. The cipV gene is 5,748 bp in length and encodes a 1,915-residue polypeptide with a calculated molecular weight of 199,496. CipV contains an N-terminal signal peptide, seven type I cohesin
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13

Phitsuwan, Moraïs, Dassa, Henrissat, and Bayer. "The Cellulosome Paradigm in An Extreme Alkaline Environment." Microorganisms 7, no. 9 (2019): 347. http://dx.doi.org/10.3390/microorganisms7090347.

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Rapid decomposition of plant biomass in soda lakes is associated with microbial activity of anaerobic cellulose-degrading communities. The alkaliphilic bacterium, Clostridium alkalicellulosi, is the single known isolate from a soda lake that demonstrates cellulolytic activity. This microorganism secretes cellulolytic enzymes that degrade cellulose under anaerobic and alkaliphilic conditions. A previous study indicated that the protein fraction of cellulose-grown cultures showed similarities in composition and size to known components of the archetypical cellulosome Clostridium thermocellum. Bi
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14

Sakka, Kazutaka, Yuka Sugihara, Sadanari Jindou, et al. "Analysis of cohesin-dockerin interactions using mutant dockerin proteins." FEMS Microbiology Letters 314, no. 1 (2010): 75–80. http://dx.doi.org/10.1111/j.1574-6968.2010.02146.x.

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15

Ding, Shi-You, Edward A. Bayer, David Steiner, Yuval Shoham, and Raphael Lamed. "A Scaffoldin of the Bacteroides cellulosolvens Cellulosome That Contains 11 Type II Cohesins." Journal of Bacteriology 182, no. 17 (2000): 4915–25. http://dx.doi.org/10.1128/jb.182.17.4915-4925.2000.

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ABSTRACT A cellulosomal scaffoldin gene, termed cipBc, was identified and sequenced from the mesophilic cellulolytic anaerobeBacteroides cellulosolvens. The gene encodes a 2,292-residue polypeptide (excluding the signal sequence) with a calculated molecular weight of 242,437. CipBc contains an N-terminal signal peptide, 11 type II cohesin domains, an internal family III cellulose-binding domain (CBD), and a C-terminal dockerin domain. Its CBD belongs to family IIIb, like that of CipV from Acetivibrio cellulolyticus but unlike the family IIIa CBDs of other clostridial scaffoldins. In contrast t
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16

Wen, Fei, Jie Sun, and Huimin Zhao. "Yeast Surface Display of Trifunctional Minicellulosomes for Simultaneous Saccharification and Fermentation of Cellulose to Ethanol." Applied and Environmental Microbiology 76, no. 4 (2009): 1251–60. http://dx.doi.org/10.1128/aem.01687-09.

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ABSTRACT By combining cellulase production, cellulose hydrolysis, and sugar fermentation into a single step, consolidated bioprocessing (CBP) represents a promising technology for biofuel production. Here we report engineering of Saccharomyces cerevisiae strains displaying a series of uni-, bi-, and trifunctional minicellulosomes. These minicellulosomes consist of (i) a miniscaffoldin containing a cellulose-binding domain and three cohesin modules, which was tethered to the cell surface through the yeast a-agglutinin adhesion receptor, and (ii) up to three types of cellulases, an endoglucanase
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17

Lytle, Betsy, and J. H. David Wu. "Involvement of Both Dockerin Subdomains in Assembly of the Clostridium thermocellum Cellulosome." Journal of Bacteriology 180, no. 24 (1998): 6581–85. http://dx.doi.org/10.1128/jb.180.24.6581-6585.1998.

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ABSTRACT Clostridium thermocellum produces an extracellular cellulase complex termed the cellulosome. It consists of a scaffolding protein, CipA, containing nine cohesin domains and a cellulose-binding domain, and at least 14 different enzymatic subunits, each containing a conserved duplicated sequence, or dockerin domain. The cohesin-dockerin interaction is responsible for the assembly of the catalytic subunits into the cellulosome structure. Each duplicated sequence of the dockerin domain contains a region bearing homology to the EF-hand calcium-binding motif. Two subdomains, each containing
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18

Pagès, Sandrine, Anne Bélaïch, Henri-Pierre Fierobe, Chantal Tardif, Christian Gaudin, and Jean-Pierre Bélaïch. "Sequence Analysis of Scaffolding Protein CipC and ORFXp, a New Cohesin-Containing Protein inClostridium cellulolyticum: Comparison of Various Cohesin Domains and Subcellular Localization of ORFXp." Journal of Bacteriology 181, no. 6 (1999): 1801–10. http://dx.doi.org/10.1128/jb.181.6.1801-1810.1999.

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ABSTRACT The gene encoding the scaffolding protein of the cellulosome fromClostridium cellulolyticum, whose partial sequence was published earlier (S. Pagès, A. Bélaı̈ch, C. Tardif, C. Reverbel-Leroy, C. Gaudin, and J.-P. Bélaı̈ch, J. Bacteriol. 178:2279–2286, 1996; C. Reverbel-Leroy, A. Bélaı̈ch, A. Bernadac, C. Gaudin, J. P. Bélaı̈ch, and C. Tardif, Microbiology 142:1013–1023, 1996), was completely sequenced. The corresponding protein, CipC, is composed of a cellulose binding domain at the N terminus followed by one hydrophilic domain (HD1), seven highly homologous cohesin domains (cohe
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19

Bule, Pedro, Vered Ruimy-Israeli, Vânia Cardoso, Edward A. Bayer, Carlos M. G. A. Fontes, and Shabir Najmudin. "Overexpression, crystallization and preliminary X-ray characterization ofRuminococcus flavefaciensscaffoldin C cohesin in complex with a dockerin from an uncharacterized CBM-containing protein." Acta Crystallographica Section F Structural Biology Communications 70, no. 8 (2014): 1061–64. http://dx.doi.org/10.1107/s2053230x14012667.

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Cellulosomes are massive cell-bound multienzyme complexes tethered by macromolecular scaffolds that coordinate the efforts of many anaerobic bacteria to hydrolyze plant cell-wall polysaccharides, which are a major untapped source of carbon and energy. Integration of cellulosomal components occursviahighly ordered protein–protein interactions between cohesin modules, located in the scaffold, and dockerin modules, found in the enzymes and other cellulosomal proteins. The proposed cellulosomal architecture forRuminococcus flavefaciensstrain FD-1 consists of a major scaffoldin (ScaB) that acts as
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20

Karpol, Alon, Yoav Barak, Raphael Lamed, Yuval Shoham, and Edward A. Bayer. "Functional asymmetry in cohesin binding belies inherent symmetry of the dockerin module: insight into cellulosome assembly revealed by systematic mutagenesis." Biochemical Journal 410, no. 2 (2008): 331–38. http://dx.doi.org/10.1042/bj20071193.

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The cellulosome is an intricate multi-enzyme complex, known for its efficient degradation of recalcitrant cellulosic substrates. Its supramolecular architecture is determined by the high-affinity intermodular cohesin–dockerin interaction. The dockerin module comprises a calcium-binding, duplicated ‘F-hand’ loop–helix motif that bears striking similarity to the EF-hand loop–helix–loop motif of eukaryotic calcium-binding proteins. In the present study, we demonstrate by progressive truncation and alanine scanning of a representative type-I dockerin module from Clostridium thermocellum, that only
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21

Levasseur, Anthony, Sandrine Pagès, Henri-Pierre Fierobe, et al. "Design and Production in Aspergillus niger of a Chimeric Protein Associating a Fungal Feruloyl Esterase and a Clostridial Dockerin Domain." Applied and Environmental Microbiology 70, no. 12 (2004): 6984–91. http://dx.doi.org/10.1128/aem.70.12.6984-6991.2004.

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ABSTRACT A chimeric enzyme associating feruloyl esterase A (FAEA) from Aspergillus niger and dockerin from Clostridium thermocellum was produced in A. niger. A completely truncated form was produced when the dockerin domain was located downstream of the FAEA (FAEA-Doc), whereas no chimeric protein was produced when the bacterial dockerin domain was located upstream of the FAEA (Doc-FAEA). Northern blot analysis showed similar transcript levels for the two constructs, indicating a posttranscriptional bottleneck for Doc-FAEA production. The sequence encoding the first 514 amino acids from A. nig
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22

Noach, Ilit, Yoav Barak, Felix Frolow, Raphael Lamed, and Edward A. Bayer. "Homology swapping of intrinsic secondary structural elements between cellulosomal types I and II cohesins and their effect on dockerin binding." Pure and Applied Chemistry 82, no. 1 (2010): 193–204. http://dx.doi.org/10.1351/pac-con-09-02-11.

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The high-affinity cohesin–dockerin interaction dictates the suprastructural assembly of the multienzyme cellulosome complex. The interaction between these two complementary families of protein modules was found to be species-specific and type-dependent. The structure of the type II cohesin module possesses additional intrinsic secondary structural elements absent in the type I cohesin, i.e., an α-helix and two singular "β-flaps". The role of these extra secondary structures in dockerin recognition was studied in this work using gene swapping, in which corresponding homologous stretches of type
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23

Salama-Alber, Orly, Maroor K. Jobby, Seth Chitayat, et al. "Atypical Cohesin-Dockerin Complex Responsible for Cell Surface Attachment of Cellulosomal Components." Journal of Biological Chemistry 288, no. 23 (2013): 16827–38. http://dx.doi.org/10.1074/jbc.m113.466672.

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The rumen bacterium Ruminococcus flavefaciens produces a highly organized multienzyme cellulosome complex that plays a key role in the degradation of plant cell wall polysaccharides, notably cellulose. The R. flavefaciens cellulosomal system is anchored to the bacterial cell wall through a relatively small ScaE scaffoldin subunit, which bears a single type IIIe cohesin responsible for the attachment of two major dockerin-containing scaffoldin proteins, ScaB and the cellulose-binding protein CttA. Although ScaB recruits the catalytic machinery onto the complex, CttA mediates attachment of the b
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24

Murashima, Koichiro, Chyi-Liang Chen, Akihiko Kosugi, Yutaka Tamaru, Roy H. Doi, and Sui-Lam Wong. "Heterologous Production of Clostridium cellulovorans engB, Using Protease-Deficient Bacillus subtilis, and Preparation of Active Recombinant Cellulosomes." Journal of Bacteriology 184, no. 1 (2002): 76–81. http://dx.doi.org/10.1128/jb.184.1.76-81.2002.

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ABSTRACT In cellulosomes produced by Clostridium spp., the high-affinity interaction between the dockerin domain and the cohesin domain is responsible for the assembly of enzymatic subunits into the complex. Thus, heterologous expression of full-length enzymatic subunits containing the dockerin domains and of the scaffolding unit is essential for the in vitro assembly of a “designer” cellulosome, or a recombinant cellulosome with a specific function. We report the preparation of Clostridium cellulovorans recombinant cellulosomes containing the enzymatic subunit EngB and the scaffolding unit, m
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25

Jindou, Sadanari, Shuichi Karita, Emi Fujino та ін. "α-Galactosidase Aga27A, an Enzymatic Component of the Clostridium josui Cellulosome". Journal of Bacteriology 184, № 2 (2002): 600–604. http://dx.doi.org/10.1128/jb.184.2.600-604.2002.

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ABSTRACT The Clostridium josui aga27A gene encodes the cellulosomal α-galactosidase Aga27A, which comprises a catalytic domain of family 27 of glycoside hydrolases and a dockerin domain responsible for cellulosome assembly. The catalytic domain is highly homologous to those of various α-galactosidases of family 27 of glycoside hydrolases from eukaryotic organisms, especially plants. The recombinant Aga27A α-galactosidase devoid of the dockerin domain preferred highly polymeric galactomannan as a substrate to small saccharides such as melibiose and raffinose.
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Tsai, Shen-Long, Jeongseok Oh, Shailendra Singh, Ruizhen Chen, and Wilfred Chen. "Functional Assembly of Minicellulosomes on the Saccharomyces cerevisiae Cell Surface for Cellulose Hydrolysis and Ethanol Production." Applied and Environmental Microbiology 75, no. 19 (2009): 6087–93. http://dx.doi.org/10.1128/aem.01538-09.

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ABSTRACT We demonstrated the functional display of a miniscaffoldin on the Saccharomyces cerevisiae cell surface consisting of three divergent cohesin domains from Clostridium thermocellum (t), Clostridium cellulolyticum (c), and Ruminococcus flavefaciens (f). Incubation with Escherichia coli lysates containing an endoglucanase (CelA) fused with a dockerin domain from C. thermocellum (At), an exoglucanase (CelE) from C. cellulolyticum fused with a dockerin domain from the same species (Ec), and an endoglucanase (CelG) from C. cellulolyticum fused with a dockerin domain from R. flavefaciens (Gf
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Mechaly, Adva, Henri-Pierre Fierobe, Anne Belaich, et al. "Cohesin-Dockerin Interaction in Cellulosome Assembly." Journal of Biological Chemistry 276, no. 13 (2001): 9883–88. http://dx.doi.org/10.1074/jbc.m009237200.

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Huang, Ya-Hui, Ching-Tsan Huang, and Ruey-Shyang Hseu. "Effects of dockerin domains onNeocallimastix frontalisxylanases." FEMS Microbiology Letters 243, no. 2 (2005): 455–60. http://dx.doi.org/10.1016/j.femsle.2005.01.008.

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29

Yao, Xingzhe, Chao Chen, Yefei Wang, et al. "Discovery and mechanism of a pH-dependent dual-binding-site switch in the interaction of a pair of protein modules." Science Advances 6, no. 43 (2020): eabd7182. http://dx.doi.org/10.1126/sciadv.abd7182.

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Many important proteins undergo pH-dependent conformational changes resulting in “on-off” switches for protein function, which are essential for regulation of life processes and have wide application potential. Here, we report a pair of cellulosomal assembly modules, comprising a cohesin and a dockerin from Clostridium acetobutylicum, which interact together following a unique pH-dependent switch between two functional sites rather than on-off states. The two cohesin-binding sites on the dockerin are switched from one to the other at pH 4.8 and 7.5 with a 180° rotation of the bound dockerin. C
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30

Ding, Shi-You, Marco T. Rincon, Raphael Lamed, et al. "Cellulosomal Scaffoldin-Like Proteins fromRuminococcus flavefaciens." Journal of Bacteriology 183, no. 6 (2001): 1945–53. http://dx.doi.org/10.1128/jb.183.6.1945-1953.2001.

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ABSTRACT Two tandem cellulosome-associated genes were identified in the cellulolytic rumen bacterium, Ruminococcus flavefaciens. The deduced gene products represent multimodular scaffoldin-related proteins (termed ScaA and ScaB), both of which include several copies of explicit cellulosome signature sequences. The scaB gene was completely sequenced, and its upstream neighbor scaAwas partially sequenced. The sequenced portion of scaAcontains repeating cohesin modules and a C-terminal dockerin domain. ScaB contains seven relatively divergent cohesin modules, two extremely long T-rich linkers, an
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31

Liu, Jin-Hao, Brent L. Selinger, Cheng-Fang Tsai, and Kuo-Jaon Cheng. "Characterization of aNeocallimastixpatriciarumxylanase gene and its product." Canadian Journal of Microbiology 45, no. 11 (1999): 970–74. http://dx.doi.org/10.1139/w99-092.

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A xylanase gene (xynC) isolated from the anaerobic ruminal fungus Neocallimastix patriciarum was characterized. The gene consists of an N-terminal catalytic domain that exhibited homology to family 11 of glycosyl hydrolases, a C-terminal cellulose binding domain (CBD) and a putative dockerin domain in between. Each domain was linked by a short linker domain rich in proline and alanine. Deletion analysis demonstrated that the CBD was essential for optimal xylanase activity of the enzyme, while the putative dockerin domain may not be required for enzyme function.Key words: xylanase, cellulose bi
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32

Venditto, Immacolata, Pedro Bule, Andrew Thompson, et al. "Expression, purification, crystallization and preliminary X-ray analysis of CttA, a putative cellulose-binding protein fromRuminococcus flavefaciens." Acta Crystallographica Section F Structural Biology Communications 71, no. 6 (2015): 784–89. http://dx.doi.org/10.1107/s2053230x15008249.

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A number of anaerobic microorganisms produce multi-modular, multi-enzyme complexes termed cellulosomes. These extracellular macromolecular nanomachines are designed for the efficient degradation of plant cell-wall carbohydrates to smaller sugars that are subsequently used as a source of carbon and energy. Cellulolytic strains from the rumens of mammals, such asRuminococcus flavefaciens, have been shown to have one of the most complex cellulosomal systems known. Cellulosome assembly requires the binding of dockerin modules located in cellulosomal enzymes to cohesin modules located in a macromol
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33

Hirano, Katsuaki, Satoshi Nihei, Hiroki Hasegawa, Mitsuru Haruki, and Nobutaka Hirano. "Stoichiometric Assembly of the Cellulosome Generates Maximum Synergy for the Degradation of Crystalline Cellulose, as Revealed byIn VitroReconstitution of the Clostridium thermocellum Cellulosome." Applied and Environmental Microbiology 81, no. 14 (2015): 4756–66. http://dx.doi.org/10.1128/aem.00772-15.

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ABSTRACTThe cellulosome is a supramolecular multienzyme complex formed by species-specific interactions between the cohesin modules of scaffoldin proteins and the dockerin modules of a wide variety of polysaccharide-degrading enzymes. Cellulosomal enzymes bound to the scaffoldin protein act synergistically to degrade crystalline cellulose. However, there have been few attempts to reconstitute intact cellulosomes due to the difficulty of heterologously expressing full-length scaffoldin proteins. We describe the synthesis of a full-length scaffoldin protein containing nine cohesin modules, CipA;
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34

Rincón, Marco T., Jennifer C. Martin, Vincenzo Aurilia, et al. "ScaC, an Adaptor Protein Carrying a Novel Cohesin That Expands the Dockerin-Binding Repertoire of the Ruminococcus flavefaciens 17 Cellulosome." Journal of Bacteriology 186, no. 9 (2004): 2576–85. http://dx.doi.org/10.1128/jb.186.9.2576-2585.2004.

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ABSTRACT A new gene, designated scaC and encoding a protein carrying a single cohesin, was identified in the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 as part of a gene cluster that also codes for the cellulosome structural components ScaA and ScaB. Phylogenetic analysis showed that the sequence of the ScaC cohesin is distinct from the sequences of other cohesins, including the sequences of R. flavefaciens ScaA and ScaB. The scaC gene product also includes at its C terminus a dockerin module that closely resembles those found in R. flavefaciens enzymes that bind to the cohesins
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35

Handelsman, Tal, Yoav Barak, David Nakar, et al. "Cohesin-dockerin interaction in cellulosome assembly: a single Asp-to-Asn mutation disrupts high-affinity cohesin-dockerin binding." FEBS Letters 572, no. 1-3 (2004): 195–200. http://dx.doi.org/10.1016/j.febslet.2004.07.040.

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36

Pagès, Sandrine, Anne Bélaïch, Jean-Pierre Bélaïch, et al. "Species-specificity of the cohesin-dockerin interaction betweenClostridium thermocellum andClostridium cellulolyticum: Prediction of specificity determinants of the dockerin domain." Proteins: Structure, Function, and Genetics 29, no. 4 (1997): 517–27. http://dx.doi.org/10.1002/(sici)1097-0134(199712)29:4<517::aid-prot11>3.0.co;2-p.

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37

Bule, Pedro, Ana Correia, Kate Cameron, et al. "Overexpression, purification, crystallization and preliminary X-ray characterization of the fourth scaffoldin A cohesin fromAcetivibrio cellulolyticusin complex with a dockerin from a family 5 glycoside hydrolase." Acta Crystallographica Section F Structural Biology Communications 70, no. 8 (2014): 1065–67. http://dx.doi.org/10.1107/s2053230x14013181.

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Cellulosomes are cell-bound multienzyme complexes secreted by anaerobic bacteria that play a crucial role in carbon turnover by degrading plant cell walls to simple sugars. Integration of cellulosomal components occursviahighly ordered protein–protein interactions between cohesin modules located in a molecular scaffold and dockerin modules found in cellulosomal enzymes.Acetivibrio cellulolyticuspossesses a complex cellulosome arrangement which is organized by a primary enzyme-binding scaffoldin (ScaA), two anchoring scaffoldins (ScaC and ScaD) and an unusual adaptor scaffoldin (ScaB). A docker
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38

Jindou, Sadanari, Akane Soda, Shuichi Karita, et al. "Cohesin-Dockerin Interactions within and betweenClostridium josuiandClostridium thermocellum." Journal of Biological Chemistry 279, no. 11 (2003): 9867–74. http://dx.doi.org/10.1074/jbc.m308673200.

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39

Venditto, Immacolata, Maria S. J. Centeno, Luis M. A. Ferreira, Carlos M. G. A. Fontes, and Shabir Najmudin. "Expression, purification and crystallization of a novel carbohydrate-binding module from theRuminococcus flavefacienscellulosome." Acta Crystallographica Section F Structural Biology Communications 70, no. 12 (2014): 1653–56. http://dx.doi.org/10.1107/s2053230x14024248.

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Anaerobic bacteria organize carbohydrate-active enzymes into a multi-component complex, the cellulosome, which degrades cellulose and hemicellulose highly efficiently. Genome sequencing ofRuminococcus flavefaciensFD-1 offers extensive information on the range and diversity of the enzymatic and structural components of the cellulosome. TheR. flavefaciensFD-1 genome encodes over 200 dockerin-containing proteins, most of which are of unknown function. One of these modular proteins comprises a glycoside hydrolase family 5 catalytic module (GH5) linked to an unclassified carbohydrate-binding module
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40

Han, Zhenlin, Bei Zhang, Yi E. Wang, Yi Y. Zuo, and Wei Wen Su. "Self-Assembled Amyloid-Like Oligomeric-Cohesin Scaffoldin for Augmented Protein Display on the Saccharomyces cerevisiae Cell Surface." Applied and Environmental Microbiology 78, no. 9 (2012): 3249–55. http://dx.doi.org/10.1128/aem.07745-11.

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ABSTRACTIn this study, a molecular self-assembly strategy to develop a novel protein scaffold for amplifying the extent and variety of proteins displayed on the surface ofSaccharomyces cerevisiaeis presented. The cellulosomal scaffolding protein cohesin and its upstream hydrophilic domain (HD) were genetically fused with the yeast Ure2p N-terminal fibrillogenic domain consisting of residues 1 to 80 (Ure2p1-80). The resulting Ure2p1-80-HD-cohesin fusion protein was successfully expressed inEscherichia colito produce self-assembled supramolecular nanofibrils that serve as a novel protein scaffol
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41

Xu, Qi, Wenchen Gao, Shi-You Ding, et al. "The Cellulosome System of Acetivibrio cellulolyticus Includes a Novel Type of Adaptor Protein and a Cell Surface Anchoring Protein." Journal of Bacteriology 185, no. 15 (2003): 4548–57. http://dx.doi.org/10.1128/jb.185.15.4548-4557.2003.

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ABSTRACT A scaffoldin gene cluster was identified in the mesophilic cellulolytic anaerobe Acetivibrio cellulolyticus. The previously described scaffoldin gene, cipV, encodes an N-terminal family 9 glycoside hydrolase, a family 3b cellulose-binding domain, seven cohesin domains, and a C-terminal dockerin. The gene immediately downstream of cipV was sequenced and designated scaB. The protein encoded by this gene has 942 amino acid residues and a calculated molecular weight of 100,358 and includes an N-terminal signal peptide, four type II cohesions, and a C-terminal dockerin. ScaB cohesins 1 and
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42

Mechaly, Adva, Henri-Pierre Fierobe, Anne Belaich, et al. "Cohesin-dockerin interaction in cellulosome assembly. A single hydroxyl group of a dockerin domain distinguishes between nonrecognition and high affinity recognition." Journal of Biological Chemistry 276, no. 22 (2001): 19678. http://dx.doi.org/10.1074/s0021-9258(19)67116-4.

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43

Kosugi, Akihiko, Koichiro Murashima, Yutaka Tamaru, and Roy H. Doi. "Cell-Surface-Anchoring Role of N-Terminal Surface Layer Homology Domains of Clostridium cellulovorans EngE." Journal of Bacteriology 184, no. 4 (2002): 884–88. http://dx.doi.org/10.1128/jb.184.4.884-888.2002.

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ABSTRACT engE, coding for endoglucanase E, one of the three major subunits of the Clostridium cellulovorans cellulosome, has been cloned and sequenced (Y. Tamaru and R. H. Doi, J. Bacteriol. 181:3270-3276, 1999). The N-terminal-half region of EngE possesses three repeated surface layer homology (SLH) domains, which are homologous to those of some bacterial S-layer proteins. Also, the C-terminal-half region consists of a catalytic domain of glycosyl hydrolase family 5 and a duplicated sequence (dockerin) for binding EngE to scaffolding protein CbpA. Our hypothesis is that the SLH domains serve
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Mechaly, Adva, Sima Yaron, Raphael Lamed, et al. "Cohesin-dockerin recognition in cellulosome assembly: Experiment versus hypothesis." Proteins: Structure, Function, and Genetics 39, no. 2 (2000): 170–77. http://dx.doi.org/10.1002/(sici)1097-0134(20000501)39:2<170::aid-prot7>3.0.co;2-h.

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45

Wang, He, Xiaomin Jiang, Yongchang Qian, and Lianghong Yin. "Constructing an Efficient Bacillus subtilis Spore Display by Using Cohesin−Dockerin Interactions." Molecules 26, no. 4 (2021): 1186. http://dx.doi.org/10.3390/molecules26041186.

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Bacillus subtilis spore display has become a field of increasing interest in the past two decades. To improve the efficiency of B. subtilis spore display, its directed modification was performed based on the cellulosome architecture by introducing onto them divergent cohesin (Coh) modules that can specifically bind to the target enzyme bearing the matching dockerins (Doc). In this study, five different pairs of cohesins and dockerins, selected from four cellulolytic microbes, were examined for their capabilities in displaying a tetrameric enzyme β-galactosidase from Bacillus stearothermophilus
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46

Pires, Ana José, Teresa Ribeiro, Andrew Thompson, et al. "Purification and crystallographic studies of a putative carbohydrate-binding module from theRuminococcus flavefaciensFD-1 endoglucanase Cel5A." Acta Crystallographica Section F Structural Biology Communications 71, no. 8 (2015): 958–61. http://dx.doi.org/10.1107/s2053230x15009784.

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Ruminant herbivores meet their carbon and energy requirements from a symbiotic relationship with cellulosome-producing anaerobic bacteria that efficiently degrade plant cell-wall polysaccharides. The assembly of carbohydrate-active enzymes (CAZymes) into cellulosomes enhances protein stability and enzyme synergistic interactions. Cellulosomes comprise diverse CAZymes displaying a modular architecture in which a catalytic domain is connected,vialinker sequences, to one or more noncatalytic carbohydrate-binding modules (CBMs). CBMs direct the appended catalytic modules to their target substrates
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47

Fierobe, Henri-Pierre, Sandrine Pagès, Anne Bélaïch, Stéphanie Champ, Doris Lexa, and Jean-Pierre Bélaïch. "Cellulosome fromClostridium cellulolyticum: Molecular Study of the Dockerin/Cohesin Interaction†." Biochemistry 38, no. 39 (1999): 12822–32. http://dx.doi.org/10.1021/bi9911740.

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48

Stahl, S. W., M. A. Nash, D. B. Fried, et al. "Single-molecule dissection of the high-affinity cohesin-dockerin complex." Proceedings of the National Academy of Sciences 109, no. 50 (2012): 20431–36. http://dx.doi.org/10.1073/pnas.1211929109.

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49

Nash, Michael A., Steven P. Smith, Carlos MGA Fontes, and Edward A. Bayer. "Single versus dual-binding conformations in cellulosomal cohesin–dockerin complexes." Current Opinion in Structural Biology 40 (October 2016): 89–96. http://dx.doi.org/10.1016/j.sbi.2016.08.002.

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50

Chen, Chao, Hongwu Yang, Jinsong Xuan, Qiu Cui, and Yingang Feng. "Resonance assignments of a cellulosomal double-dockerin from Clostridium thermocellum." Biomolecular NMR Assignments 13, no. 1 (2018): 97–101. http://dx.doi.org/10.1007/s12104-018-9859-7.

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