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Academic literature on the topic 'POTRA'

Author: Grafiati
Published: 4 June 2021
Last updated: 18 February 2022

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Journal articles on the topic "POTRA"

1

Bertran, Ramon, Marc Gonzàlez, Xavier Martorell, Nacho Navarro, and Eduard Ayguadé. "POTRA." ACM SIGMETRICS Performance Evaluation Review 40, no. 1 (2012): 427–28. http://dx.doi.org/10.1145/2318857.2254827.

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2

Grass, Susan, Katherine A. Rempe, and Joseph W. St. Geme. "Structural Determinants of the Interaction between the TpsA and TpsB Proteins in the Haemophilus influenzae HMW1 Two-Partner Secretion System." Journal of Bacteriology 197, no. 10 (2015): 1769–80. http://dx.doi.org/10.1128/jb.00039-15.

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ABSTRACTThe two-partner secretion (TPS) pathway in Gram-negative bacteria consists of a TpsA exoprotein and a cognate TpsB outer membrane pore-forming translocator protein. Previous work has demonstrated that the TpsA protein contains an N-terminal TPS domain that plays an important role in targeting the TpsB protein and is required for secretion. The nontypeableHaemophilus influenzaeHMW1 and HMW2 adhesins are homologous proteins that are prototype TpsA proteins and are secreted by the HMW1B and HMW2B TpsB proteins. In the present study, we sought to define the structural determinants of HMW1 interaction with HMW1B during the transport process and while anchored to the bacterial surface. Modeling of HMW1B revealed an N-terminal periplasmic region that contains two polypeptide transport-associated (POTRA) domains and a C-terminal membrane-localized region that forms a pore. Biochemical studies demonstrated that HMW1 engages HMW1B via interaction between the HMW1 TPS domain and the HMW1B periplasmic region, specifically, the predicted POTRA1 and POTRA2 domains. Subsequently, HMW1 is shuttled to the HMW1B pore, facilitated by the N-terminal region, the middle region, and the NPNG motif in the HMW1 TPS domain. Additional analysis revealed that the interaction between HMW1 and HMW1B is highly specific and is dependent upon the POTRA domains and the pore-forming domain of HMW1B. Further studies established that tethering of HMW1 to the surface-exposed region of HMW1B is dependent upon the external loops of HMW1B formed by residues 267 to 283 and residues 324 to 330. These observations may have broad relevance to proteins secreted by the TPS pathway.IMPORTANCESecretion of HMW1 involves a recognition event between the extended form of the HMW1 propiece and the HMW1B POTRA domains. Our results identify specific interactions between the HMW1 propiece and the periplasmic HMW1B POTRA domains. The results also suggest that the process of HMW1 translocation involves at least two discrete steps, including initial interaction between the HMW1 propiece and the HMW1B POTRA domains and then a separate translocation event. We have also discovered that the HMW1B pore itself appears to influence the translocation process. These observations extend our knowledge of the two-partner secretion system and may be broadly relevant to other proteins secreted by the TPS pathway.
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3

O’Neil, Patrick K., Lynn G. L. Richardson, Yamuna D. Paila, et al. "The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts." Proceedings of the National Academy of Sciences 114, no. 24 (2017): E4868—E4876. http://dx.doi.org/10.1073/pnas.1621179114.

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Protein trafficking across membranes is an essential function in cells; however, the exact mechanism for how this occurs is not well understood. In the endosymbionts, mitochondria and chloroplasts, the vast majority of proteins are synthesized in the cytoplasm as preproteins and then imported into the organelles via specialized machineries. In chloroplasts, protein import is accomplished by the TOC (translocon on the outer chloroplast membrane) and TIC (translocon on the inner chloroplast membrane) machineries in the outer and inner envelope membranes, respectively. TOC mediates initial recognition of preproteins at the outer membrane and includes a core membrane channel, Toc75, and two receptor proteins, Toc33/34 and Toc159, each containing GTPase domains that control preprotein binding and translocation. Toc75 is predicted to have a β-barrel fold consisting of an N-terminal intermembrane space (IMS) domain and a C-terminal 16-stranded β-barrel domain. Here we report the crystal structure of the N-terminal IMS domain of Toc75 from Arabidopsis thaliana, revealing three tandem polypeptide transport-associated (POTRA) domains, with POTRA2 containing an additional elongated helix not observed previously in other POTRA domains. Functional studies show an interaction with the preprotein, preSSU, which is mediated through POTRA2-3. POTRA2-3 also was found to have chaperone-like activity in an insulin aggregation assay, which we propose facilitates preprotein import. Our data suggest a model in which the POTRA domains serve as a binding site for the preprotein as it emerges from the Toc75 channel and provide a chaperone-like activity to prevent misfolding or aggregation as the preprotein traverses the intermembrane space.
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4

Molloy, Sheilagh. "POTRA domains close up." Nature Reviews Microbiology 5, no. 10 (2007): 747. http://dx.doi.org/10.1038/nrmicro1756.

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5

Stroud, David A., Thomas Becker, Jian Qiu та ін. "Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex". Molecular Biology of the Cell 22, № 16 (2011): 2823–33. http://dx.doi.org/10.1091/mbc.e11-02-0148.

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The mitochondrial outer membrane contains proteinaceous machineries for the translocation of precursor proteins. The sorting and assembly machinery (SAM) is required for the insertion of β‑barrel proteins into the outer membrane. Sam50 is the channel-forming core subunit of the SAM complex and belongs to the BamA/Sam50/Toc75 family of proteins that have been conserved from Gram-negative bacteria to mitochondria and chloroplasts. These proteins contain one or more N-terminal polypeptide transport-associated (POTRA) domains. POTRA domains can bind precursor proteins, however, different views exist on the role of POTRA domains in the biogenesis of β-barrel proteins. It has been suggested that the single POTRA domain of mitochondrial Sam50 plays a receptor-like function at the SAM complex. We established a system to monitor the interaction of chemical amounts of β-barrel precursor proteins with the SAM complex of wild-type and mutant yeast in organello. We report that the SAM complex lacking the POTRA domain of Sam50 efficiently binds β-barrel precursors, but is impaired in the release of the precursors. These results indicate the POTRA domain of Sam50 is not essential for recognition of β-barrel precursors but functions in a subsequent step to promote the release of precursor proteins from the SAM complex.
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6

Dong, Shishang, Hongguan Chu, Kangning Wen та ін. "Crystallization and X-ray analysis of Borrelia burgdorferi β-barrel assembly machinery A". Acta Crystallographica Section F Structural Biology Communications 76, № 6 (2020): 235–40. http://dx.doi.org/10.1107/s2053230x20006196.

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Mitochondria, chloroplasts and several species of bacteria have outer membrane proteins (OMPs) that perform many essential biological functions. The β-barrel assembly machinery (BAM) complex is one of the OMPs of Borrelia burgdorferi, the pathogenic spirochete that causes Lyme disease, and its BamA component (BbBamA) includes a C-terminal β-barrel domain and five N-terminal periplasmic polypeptide-transport-associated (POTRA) domains, which together perform a central transport function. In the current work, the production, crystallization and X-ray analysis of the three N-terminal POTRA domains of BbBamA (BbBamA-POTRA P1–P3; residues 30–273) were carried out. The crystals of BbBamA-POTRA P1–P3 belonged to space group P21, with unit-cell parameters a = 45.353, b = 111.538, c = 64.376 Å, β = 99.913°. The Matthews coefficient was calculated to be 2.92 Å3 Da−1, assuming the presence of two molecules per asymmetric unit, and the corresponding solvent content was 57.9%. Owing to the absence of an ideal homology model, numerous attempts to solve the BbBamA-POTRA P1–P3 structure using molecular replacement (MR) failed. In order to solve the structure, further trials using selenomethionine derivatization are currently being carried out.
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7

Lotfi, Taher, Stanford Shateyi, and Sommayeh Hadadi. "Potra-Pták Iterative Method with Memory." ISRN Mathematical Analysis 2014 (January 22, 2014): 1–6. http://dx.doi.org/10.1155/2014/697642.

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The problem is to extend the method proposed by Soleymani et al. (2012) to a method with memory. Following this aim, a free parameter is calculated using Newton’s interpolatory polynomial of the third degree. So the R-order of convergence is increased from 4 to 6 without any new function evaluations. Numerically the extended method is examined along with comparison to some existing methods with the similar properties.
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8

Rossi, R., J. M. Silva Filho, M. S. Palhares, M. M. Silva, R. A. Martins, and C. L. A. Silva. "Efeito da categoria reprodutiva sobre a fertilidade de éguas inseminadas com sêmen asinino diluído e resfriado a 5ºC por 12 horas de armazenamento." Arquivo Brasileiro de Medicina Veterinária e Zootecnia 66, no. 6 (2014): 1655–61. http://dx.doi.org/10.1590/1678-7248.

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Estudou-se o efeito da categoria reprodutiva sobre a fertilidade de éguas inseminadas com sêmen asinino diluído, resfriado e armazenado. Os ciclos foram acompanhados por palpação retal e rufiação, sendo as inseminações realizadas às terças, quintas e sábados, a partir da detecção de um folículo de 3,0 a 3,5cm de diâmetro, em um dos ovários, até a ovulação. O sêmen de cinco jumentos da raça Pêga foi diluído nos diluidores de leite em pó desnatado-glicose ou glicina-gema de ovo, resfriado a 5ºC e armazenado por 12 horas, sendo a dose inseminante de 400 x 106espermatozoides móveis (no momento da diluição final, pré-resfriamento) depositada no corpo do útero. O diagnóstico de gestação foi realizado por meio de palpação transretal, rufiação e ultrassonografia, realizada a cada 14 dias. Os resultados de 195 ciclos, referentes a 141 éguas, foram agrupados de acordo com a categoria reprodutiva a que pertenciam: potra, égua solteira, égua parida e no "cio do potro". As taxas de concepção, ao primeiro ciclo, foram de 60,00%, 48,28%, 75,00% e 47,17% e, após quatro ciclos, de 61,54%, 47,13%, 54,76% e 47,17%, na mesma ordem para as categorias descritas anteriormente. A categoria reprodutiva não teve efeito (P>0,05) sobre a fertilidade das éguas inseminadas com sêmen asinino resfriado, sendo as potras, éguas solteiras, éguas paridas e no "cio do potro" igualmente eficientes para o uso na reprodução.
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9

Souza, Luiz Antonio Farani de, Emerson Vitor Castelani, and Wesley Vagner Inês Shirabayashi. "Adaptation of the Newton-Raphson and Potra-Pták methods for the solution of nonlinear systems." Semina: Ciências Exatas e Tecnológicas 42, no. 1 (2021): 63. http://dx.doi.org/10.5433/1679-0375.2021v42n1p63.

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In this paper we adapt the Newton-Raphson and Potra-Pták algorithms by combining them with the modified Newton-Raphson method by inserting a condition. Problems of systems of sparse nonlinear equations are solved the algorithms implemented in Matlab® environment. In addition, the methods are adapted and applied to space trusses problems with geometric nonlinear behavior. Structures are discretized by the Finite Element Positional Method, and nonlinear responses are obtained in an incremental and iterative process using the Linear Arc-Length path-following technique. For the studied problems, the proposed algorithms had good computational performance reaching the solution with shorter processing time and fewer iterations until convergence to a given tolerance, when compared to the standard algorithms of the Newton-Raphson and Potra-Pták methods.
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10

Pereira, Andrielli Trentim, Ana Paula Maurique Pereira, Inácio Manassi da Conceição Brandolt, et al. "Linfoma multicêntrico de Células T em uma potra Crioula." Semina: Ciências Agrárias 41, no. 2 (2020): 725–30. http://dx.doi.org/10.5433/1679-0359.2020v41n2p725.

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