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Relevant bibliographies by topics / Protein import into mitochondria

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Academic literature on the topic 'Protein import into mitochondria'

Author: Grafiati

Published: 2 June 2025

Last updated: 31 July 2025

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Journal articles on the topic "Protein import into mitochondria"

1

Asai, Takeyoshi, Takashi Takahashi, Masatoshi Esaki, et al. "Reinvestigation of the Requirement of Cytosolic ATP for Mitochondrial Protein Import." Journal of Biological Chemistry 279, no. 19 (2004): 19464–70. http://dx.doi.org/10.1074/jbc.m401291200.

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Protein import into mitochondria requires the energy of ATP hydrolysis inside and/or outside mitochondria. Although the role of ATP in the mitochondrial matrix in mitochondrial protein import has been extensively studied, the role of ATP outside mitochondria (external ATP) remains only poorly characterized. Here we developed a protocol for depletion of external ATP without significantly reducing the import competence of precursor proteins synthesizedin vitrowith reticulocyte lysate. We tested the effects of external ATP on the import of various precursor proteins into isolated yeast mitochondr

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Haastrup, Mary Oluwadamilola, Kunwar Somesh Vikramdeo, Seema Singh, Ajay Pratap Singh, and Santanu Dasgupta. "The Journey of Mitochondrial Protein Import and the Roadmap to Follow." International Journal of Molecular Sciences 24, no. 3 (2023): 2479. http://dx.doi.org/10.3390/ijms24032479.

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Mitochondria are double membrane-bound organelles that play critical functions in cells including metabolism, energy production, regulation of intrinsic apoptosis, and maintenance of calcium homeostasis. Mitochondria are fascinatingly equipped with their own genome and machinery for transcribing and translating 13 essential proteins of the oxidative phosphorylation system (OXPHOS). The rest of the proteins (99%) that function in mitochondria in the various pathways described above are nuclear-transcribed and synthesized as precursors in the cytosol. These proteins are imported into the mitocho

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Ahmed, Afsar U., Peter L. Beech, Sui T. Lay, Paul R. Gilson, and Paul R. Fisher. "Import-Associated Translational Inhibition: Novel In Vivo Evidence for Cotranslational Protein Import into Dictyostelium discoideum Mitochondria." Eukaryotic Cell 5, no. 8 (2006): 1314–27. http://dx.doi.org/10.1128/ec.00386-05.

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ABSTRACT To investigate protein import into the mitochondria of Dictyostelium discoideum, green fluorescent protein (GFP) was fused as a reporter protein either to variable lengths of the N-terminal region of chaperonin 60 (the first 23, 40, 80, 97, and 150 amino acids) or to the mitochondrial targeting sequence of DNA topoisomerase II. The fusion proteins were expressed in AX2 cells under the actin-15 promoter. Fluorescence images of GFP transformants confirmed that Dictyostelium chaperonin 60 is a mitochondrial protein. The level of the mitochondrially targeted GFP fusion proteins was unexpe

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Craig, E. E., and D. A. Hood. "Influence of aging on protein import into cardiac mitochondria." American Journal of Physiology-Heart and Circulatory Physiology 272, no. 6 (1997): H2983—H2988. http://dx.doi.org/10.1152/ajpheart.1997.272.6.h2983.

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This study was undertaken to determine whether age-related changes in the content and composition of cardiac mitochondria could be due, in part, to alterations in mitochondrial protein import. Precursor proteins malate dehydrogenase and ornithine carbamoyltransferase were synthesized by in vitro transcription and translation and were incubated with mitochondria isolated from the hearts of young (4-mo), old (22-mo), and senescent (28-mo) rats. Mitochondria from senescent animals exhibited a twofold higher import rate of both precursors into the matrix compartment compared with mitochondria from

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Althoff, Lukas F. J., Markus M. Kramer, Benjamin Bührer, Denise Gaspar, and Gerald Radziwill. "Optogenetic Control of the Mitochondrial Protein Import in Mammalian Cells." Cells 13, no. 19 (2024): 1671. http://dx.doi.org/10.3390/cells13191671.

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Mitochondria provide cells with energy and regulate the cellular metabolism. Almost all mitochondrial proteins are nuclear-encoded, translated on ribosomes in the cytoplasm, and subsequently transferred to the different subcellular compartments of mitochondria. Here, we developed OptoMitoImport, an optogenetic tool to control the import of proteins into the mitochondrial matrix via the presequence pathway on demand. OptoMitoImport is based on a two-step process: first, light-induced cleavage by a TEV protease cuts off a plasma membrane-anchored fusion construct in close proximity to a mitochon

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Kawai, Akemi, Shuh-ichi Nishikawa, Aiko Hirata, and Toshiya Endo. "Loss of the mitochondrial Hsp70 functions causes aggregation of mitochondria in yeast cells." Journal of Cell Science 114, no. 19 (2001): 3565–74. http://dx.doi.org/10.1242/jcs.114.19.3565.

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Ssc1p, a member of the Hsp70 family in the mitochondrial matrix of budding yeast, mediates protein import into mitochondria and prevents irreversible aggregation of proteins in the mitochondrial matrix during folding/assembly or at elevated temperature. Here, we show that functional inactivation of the mitochondrial Hsp70 system causes aggregation of mitochondria. When temperature-sensitive mitochondrial Hsp70 mutant cells were incubated at restrictive temperature, a tubular network of mitochondria was collapsed to form aggregates. Inhibition of protein synthesis in the cytosol did not suppres

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Seo, Young Ah, Veronica Lopez, and Shannon L. Kelleher. "A histidine-rich motif mediates mitochondrial localization of ZnT2 to modulate mitochondrial function." American Journal of Physiology-Cell Physiology 300, no. 6 (2011): C1479—C1489. http://dx.doi.org/10.1152/ajpcell.00420.2010.

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Female reproductive tissues such as mammary glands, ovaries, uterus, and placenta are phenotypically dynamic, requiring tight integration of bioenergetic and apoptotic mechanisms. Mitochondrial zinc (Zn) pools have emerged as a central player in regulating bioenergetics and apoptosis. Zn must first be imported into mitochondria to modulate mitochondrion-specific functions; however, mitochondrial Zn import mechanisms have not been identified. Here we documented that the Zn transporter ZnT2 is associated with the inner mitochondrial membrane and acts as an auxiliary Zn importer into mitochondria

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Endo, Toshiya, and Haruka Sakaue. "Multifaceted roles of porin in mitochondrial protein and lipid transport." Biochemical Society Transactions 47, no. 5 (2019): 1269–77. http://dx.doi.org/10.1042/bst20190153.

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Abstract Mitochondria are essential eukaryotic organelles responsible for primary cellular energy production. Biogenesis, maintenance, and functions of mitochondria require correct assembly of resident proteins and lipids, which require their transport into and within mitochondria. Mitochondrial normal functions also require an exchange of small metabolites between the cytosol and mitochondria, which is primarily mediated by a metabolite channel of the outer membrane (OM) called porin or voltage-dependent anion channel. Here, we describe recently revealed novel roles of porin in the mitochondr

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Ilkow, Carolina S., Daniel Weckbecker, Woo Jung Cho, et al. "The Rubella Virus Capsid Protein Inhibits Mitochondrial Import." Journal of Virology 84, no. 1 (2009): 119–30. http://dx.doi.org/10.1128/jvi.01348-09.

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ABSTRACT The rubella virus (RV) capsid is an RNA-binding protein that functions in nucleocapsid assembly at the Golgi complex, the site of virus budding. In addition to its role in virus assembly, pools of capsid associate with mitochondria, a localization that is not consistent with virus assembly. Here we examined the interaction of capsid with mitochondria and showed that this viral protein inhibits the import and processing of mitochondrial precursor proteins in vitro. Moreover, RV-infected cells were found to contain lower intramitochondrial levels of matrix protein p32. In addition to in

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Hamilton, James, Tatiana Brustovetsky, Rajesh Khanna, and Nickolay Brustovetsky. "Mutant huntingtin does not cross the mitochondrial outer membrane." Human Molecular Genetics 29, no. 17 (2020): 2962–75. http://dx.doi.org/10.1093/hmg/ddaa185.

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Abstract Mutant huntingtin (mHTT) is associated with mitochondria, but the exact mitochondrial location of mHTT has not been definitively established. Recently, it was reported that mHTT is present in the intermembrane space and inhibits mitochondrial protein import by interacting with TIM23, a major component of mitochondrial protein import machinery, but evidence for functional ramifications were not provided. We assessed mHTT location using synaptic and nonsynaptic mitochondria isolated from brains of YAC128 mice and subjected to alkali treatment or limited trypsin digestion. Mitochondria w

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Dissertations / Theses on the topic "Protein import into mitochondria"

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Craig, Elaine. "Protein import into cardiac mitochondria." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp02/NQ39261.pdf.

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Wilpe, Sandra van. "Protein import into yeast mitochondria." [S.l. : Amsterdam : s.n.] ; Universiteit van Amsterdam [Host], 2000. http://dare.uva.nl/document/56852.

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Cargill, Holly Beth. "Assaying protein import into mitochondria using fluorescence spectroscopy." Texas A&M University, 2003. http://hdl.handle.net/1969.1/3971.

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Most proteins residing in the mitochondrial matrix are synthesized in the cytosol and post-translationally imported into the mitochondrial matrix. The matrix-targeted preproteins traverse the outer mitochondrial membrane (OM) via the Translocase of the Outer Membrane (TOM) complex, and the inner mitochondrial membrane (IM) via the Translocase of the Inner Membrane 23 (TIM23) complex. A novel system was set up to examine the import of matrix-targeted preproteins into mitochondria using fluorescence spectroscopy. The fluorescent probe 6-(7-nitrobenz-2-oxa-1,3-diazol-4- yl)aminohexanoic acid (NBD

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Schleiff, Enrico. "Protein import into mitochondria, a study on hTom20." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0017/NQ50256.pdf.

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Schleiff, Enrico. "Protein import into mitochondria : a study on hTom20." Thesis, McGill University, 1998. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=37570.

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Tom20 is a major receptor for protein translocation located on the outer mitochondrial membrane. This protein is a member of a multicomponent complex and is found to stimulate import of all classes of preproteins. In here, the biochemical and biophysical characterization of the human homologue will be presented. A new binding method was developed in order to study the properties of the protein. The receptor contains two distinct domains for recognition of different classes of preproteins and both domains show different binding characteristics. The interaction with terminal targeting sequences

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Purdue, Paul Edward. "Nuclear genes and protein import into maize mitochondria." Thesis, University of Edinburgh, 1988. http://hdl.handle.net/1842/12812.

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Liu, Xingquan 1959. "Import of proteins into mitochondria : biogenesis of the uncoupling protein and identification of a mitochondrial signal peptide binding protein." Thesis, McGill University, 1989. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=74310.

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The inner membrane uncoupling protein (UCP) of rat brown fat mitochondria has been imported into rat heart mitochondria in vitro. Two import signals have been detected in UCP. The intrinsic membrane insertion information of UCP has been abrogated by a signal sequence fused in front of UCP, resulting in the rerouting of UCP into the matrix. Following removal of the signal sequence from the hybrid protein, the UCP moiety remained in the soluble matrix space indicating an incompatibility of UCP insertion into the inner membrane from the matrix side.<br>An integral mitochondrial membrane protein (

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Ross, Katharina. "The mitochondrial protein import machinery." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2009. http://dx.doi.org/10.18452/16024.

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Menschliche Mitochondrien enthalten etwa 1500 bis 2000 Proteine. Die meisten dieser Proteine werden im Zellkern kodiert und im Zytoplasma synthetisiert, und müssen daher über eine spezielle Maschinerie in die Mitochondrien transportiert werden. Obwohl mittlerweile viele Details über die Wirkungsweise dieser Proteinschleusen bekannt sind, wurden einige wichtige Aspekte des Proteinimports noch nicht ausreichend untersucht. Zum einen ist nicht bekannt, ob die einzelnen Importkomplexe einen Einfluss auf die mitochondrienvermittelte Apoptose haben. Weiterhin ist offen, welche genaue Rolle der Mitoc

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Takahashi, Mark. "Protein import into intermyofibrillar and subsarcolemmal skeletal muscle mitochondria." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq22932.pdf.

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Schusdziarra, Christina. "Functional characterization of MCJ in the protein import into human mitochondria." Diss., Ludwig-Maximilians-Universität München, 2014. http://nbn-resolving.de/urn:nbn:de:bvb:19-177136.

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Books on the topic "Protein import into mitochondria"

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Knorpp, Carina. Plant mitochondrial biogenesis: Protein sorting, import, processing and degradation. Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, 1995.

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O'Regan, Seamus G. Cytosolic factors involved in the import of precursor proteins by plant mitochondria. University College Dublin, 1996.

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Sirk, Daniel. The effects of sub-lethal A[Beta](25-25) on mitochondrial protein import and degradation in differentiated PC12 cells. National Library of Canada, 2002.

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Cleary, Suzanne Patricia. Protein targeting to mitochondria and chloroplasts. typescript, 2000.

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service), ScienceDirect (Online, ed. Mitochondrial function: Mitochondrial protein kinases, protein phosphatases and mitochondrial diseases. Academic Press/Elsevier, 2009.

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Wadia, J. S. Changes in mitochondrial protein import during apoptosis. 2002.

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Phan, Nam. Stress induced modulation of mitochondrial protein import in differentiated PC12 cells: The role of Tom20. 2006.

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8

Protein Targeting to Mitochondria. Elsevier, 1996. http://dx.doi.org/10.1016/s1569-2558(09)x6001-7.

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Hartl, F. U. Protein Targeting to Mitochondria. Elsevier Science & Technology Books, 1997.

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Zimmermann, Richard, and Sven Lang, eds. Mechanisms of ER Protein Import. MDPI, 2022. http://dx.doi.org/10.3390/books978-3-0365-4093-1.

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Book chapters on the topic "Protein import into mitochondria"

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Glaser, Elzbieta, and James Whelan. "Protein Import into Plant Mitochondria." In Plant Mitochondria. Springer New York, 2010. http://dx.doi.org/10.1007/978-0-387-89781-3_11.

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Hannavy, K., and G. Schatz. "Protein import into mitochondria." In Biochemistry of Cell Membranes. Birkhäuser Basel, 1995. http://dx.doi.org/10.1007/978-3-0348-9057-1_5.

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Becker, D., U. K. Seibold, and W. Voos. "Mitochondrial Protein Import in Fungi and Animals." In Plant Mitochondria. Springer New York, 2010. http://dx.doi.org/10.1007/978-0-387-89781-3_12.

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Whelan, James, and Enrico Schleiff. "Protein Targeting and Import." In Plant Mitochondria: From Genome to Function. Springer Netherlands, 2004. http://dx.doi.org/10.1007/978-1-4020-2400-9_3.

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Chaumont, François, and Marc Boutry. "Protein Import into Plant Mitochondria." In The molecular biology of plant mitochondria. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0163-9_6.

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Mokranjac, Dejana, and Walter Neupert. "Protein Import Into Isolated Mitochondria." In Methods in Molecular Biology. Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-365-3_20.

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Chaumont, François, and Marc Boutry. "Protein Import into Plant Mitochondria." In Plant Molecular Biology 2. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3304-7_60.

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Horwich, A. L., M. Cheng, A. West, and R. A. Pollock. "Mitochondrial Protein Import." In Current Topics in Microbiology and Immunology. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76389-2_1.

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Dolezal, Pavel, Abhijith Makki, and Sabrina D. Dyall. "Protein Import into Hydrogenosomes and Mitosomes." In Hydrogenosomes and Mitosomes: Mitochondria of Anaerobic Eukaryotes. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-17941-0_3.

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Schatz, Gottfried. "Import, Folding and Degradation of Proteins by Mitochondria." In Lipid and Protein Traffic. Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-51463-0_1.

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Conference papers on the topic "Protein import into mitochondria"

1

Balan, Ion, Peter Surai, Monica Marin, et al. "Morfofuncționalitatea mitocondrială în evoluția spermatogenezei la mamifere." In "Fiziologia şi sănătatea", congresul fiziologilor. Bulletin of the Academy of Sciences of Moldova. Medical Sciences, 2025. https://doi.org/10.52692/cfzl2024.10.

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In spermatogenesis, mitochondria are particularly important for the development and maintenance of germ cells and the production of healthy gametes. Deficiencies in these processes lead to mitochondrial dysfunction and abnormal spermatogenesis. The classical roles of mitochondria in energy production, metabolism and apoptosis have been well defined, but they also have various other functions. Mitochondria are also involved in testosterone production, regulating proton secretion in the lumen to maintain an acidic state in the epididymis, and condensing sperm DNA. In the available literature on

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Konstantinov, Yu M., M. V. Koulintchenko, E. S. Klimenko, N. A. Bolotova, V. I. Tarasenko, and V. N. Shmakov. "STUDYING OF DNA IMPORT FACTORS IN PLANT MITOCHONDRIA." In The Second All-Russian Scientific Conference with international participation "Regulation Mechanisms of Eukariotic Cell Organelle Functions". SIPPB SB RAS, 2018. http://dx.doi.org/10.31255/978-5-94797-318-1-55-57.

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Klimenko, E. S., V. N. Shmakov, N. A. Bolotova, et al. "STUDY OF DNA IMPORT INTO PLANT MITOCHONDRIA USING THE RECONSTRUCTION METHOD." In The All-Russian Scientific Conference with International Participation and Schools of Young Scientists "Mechanisms of resistance of plants and microorganisms to unfavorable environmental". SIPPB SB RAS, 2018. http://dx.doi.org/10.31255/978-5-94797-319-8-1272-1275.

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Konstantinov, Y. M., Т. А. Bolotova, A. Dietrich, F. Weber-Lotfi, and M. V. Koulintchenko. "STUDYING OF DIFFERENT LENGTH AND STRUCTURE DNA IMPORT INTO PLANT MITOCHONDRIA." In The All-Russian Scientific Conference with International Participation and Schools of Young Scientists "Mechanisms of resistance of plants and microorganisms to unfavorable environmental". SIPPB SB RAS, 2018. http://dx.doi.org/10.31255/978-5-94797-319-8-1276-1279.

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Tarasenko, V. I., T. A. Bolotova, M. V. Koulintchenko, and Y. M. Konstantinov. "STUDY OF DNA IMPORT INTO MITOCHONDRIA IN VIVO USING ARABIDOPSIS PROTOPLASTS." In The All-Russian Scientific Conference with International Participation and Schools of Young Scientists "Mechanisms of resistance of plants and microorganisms to unfavorable environmental". SIPPB SB RAS, 2018. http://dx.doi.org/10.31255/978-5-94797-319-8-1385-1387.

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Tarasenko, V. I., M. V. Kulinchenko, E. S. Klimenko, et al. "Import of DNA into plant mitochondria: relationship with genetic and physiological processes." In IX Congress of society physiologists of plants of Russia "Plant physiology is the basis for creating plants of the future". Kazan University Press, 2019. http://dx.doi.org/10.26907/978-5-00130-204-9-2019-424.

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Bolotova, T. A., V. I. Tarasenko, Y. M. Konstantinov, and M. V. Koulintchenko. "STUDY OF ARABIDOPSIS MITOCHONDRIAL MEMBRANE PROTEINS ROLE IN DNA IMPORT." In The Second All-Russian Scientific Conference with international participation "Regulation Mechanisms of Eukariotic Cell Organelle Functions". SIPPB SB RAS, 2018. http://dx.doi.org/10.31255/978-5-94797-318-1-14-16.

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Nakamura, Yasuyuki, Masayuki Tsuneki, Makoto Yamamoto, and Hirofumi Arakawa. "Abstract 3316: Mieap, the mitochondria-eating protein, induces cell death by eating unhealthy mitochondria." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-3316.

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Neklesova, M. V., S. A. Silonov, E. Y. Smirnov, et al. "THE ROLE OF PROMYELOCYTIC LEUKEMIA PROTEIN IN MAMMALIAN INTRACELLULAR CALCIUM TRANSPORT." In XI МЕЖДУНАРОДНАЯ КОНФЕРЕНЦИЯ МОЛОДЫХ УЧЕНЫХ: БИОИНФОРМАТИКОВ, БИОТЕХНОЛОГОВ, БИОФИЗИКОВ, ВИРУСОЛОГОВ, МОЛЕКУЛЯРНЫХ БИОЛОГОВ И СПЕЦИАЛИСТОВ ФУНДАМЕНТАЛЬНОЙ МЕДИЦИНЫ. IPC NSU, 2024. https://doi.org/10.25205/978-5-4437-1691-6-262.

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Promyelocytic leukemia protein (PML) is known to be involved in the regulation of calcium ion transport from the endoplasmic reticulum (ER) to mitochondria. In this paper, the effect of PML gene knockout in HeLa cells on intracellular transport of calcium ions was investigated. It has been shown that PML knockout reduces the basal level of Са2+, intensifies the Са2+ release from ER, increases the intake of Са2+ into mitochondria and complicates the depolarization of mitochondria.

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Nakamura, Yasuyuki, Naoki Ikari, and Hirofumi Arakawa. "Abstract 697: Degradation of cancer mitochondria by the mitochondria-eating protein induces iron-dependent cancer cell death." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-697.

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Reports on the topic "Protein import into mitochondria"

1

Grubbs, Kyle, Nicholas K. Gabler, Jack C. M. Dekkers, Elisabeth J. Huff-Lonergan, and Steven M. Lonergan. Selection for Residual Feed Intake Alters the Protein Profile of the Mitochondria in Pigs. Iowa State University, 2014. http://dx.doi.org/10.31274/ans_air-180814-1206.

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Citovsky, Vitaly, and Yedidya Gafni. Nuclear Import of the Tomato Yellow Curl Leaf Virus in Tomato Plants. United States Department of Agriculture, 1994. http://dx.doi.org/10.32747/1994.7568765.bard.

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Tomato yellow leaf curl geminivirus (TYLCV) is a major pathogen of cultivated tomato, causing up to 100% crop loss in many parts of the world. In Israel the disease is well known and has an economic significance. In recent years viral symptoms were found in countries of the "New World" and since 1997, in Florida. Surprisingly, little is known about the molecular mechanisms of TYLCV interaction with the host plant cells. This proposal was aimed at expanding our understanding of the molecular mechanisms by which TYLCV enters the host cell nucleus. The main objective was to elucidate the TYLCV pr

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Citovsky, Vitaly, and Yedidya Gafni. Viral and Host Cell Determinants of Nuclear Import and Export of the Tomato Yellow Leaf Curl Virus in Tomato Plants. United States Department of Agriculture, 2002. http://dx.doi.org/10.32747/2002.7585200.bard.

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Tomato yellow leaf curl geminivirus (TYLCV) is a major pathogen of cultivated tomato, causing up to 100% crop loss in many parts of the world. In Israel, where TYLCV epidemics have been recorded since the 1960' s, this viral disease is well known and has been of economic significance ever since. In recent years, TYLCV outbreaks also occurred in the "New World" - Cuba, The Dominican Republic, and in the USA, in Florida, Georgia and Louisiana. Thus, TYLCV substantially hinders tomato growth throughout the world. Surprisingly, however, little is known about the molecular mechanisms of TYLCV inter

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Brosh, Arieh, Gordon Carstens, Kristen Johnson, et al. Enhancing Sustainability of Cattle Production Systems through Discovery of Biomarkers for Feed Efficiency. United States Department of Agriculture, 2011. http://dx.doi.org/10.32747/2011.7592644.bard.

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Feed inputs represent the largest variable cost of producing meat and milk from ruminant animals. Thus, strategies that improve the efficiency of feed utilization are needed to improve the global competitiveness of Israeli and U.S. cattle industries, and mitigate their environmental impact through reductions in nutrient excretions and greenhouse gas emissions. Implementation of innovative technologies that will enhance genetic merit for feed efficiency is arguably one of the most cost-effective strategies to meet future demands for animal-protein foods in an environmentally sustainable manner.

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Tzfira, Tzvi, Michael Elbaum, and Sharon Wolf. DNA transfer by Agrobacterium: a cooperative interaction of ssDNA, virulence proteins, and plant host factors. United States Department of Agriculture, 2005. http://dx.doi.org/10.32747/2005.7695881.bard.

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Agrobacteriumtumefaciensmediates genetic transformation of plants. The possibility of exchanging the natural genes for other DNA has led to Agrobacterium’s emergence as the primary vector for genetic modification of plants. The similarity among eukaryotic mechanisms of nuclear import also suggests use of its active elements as media for non-viral genetic therapy in animals. These considerations motivate the present study of the process that carries DNA of bacterial origin into the host nucleus. The infective pathway of Agrobacterium involves excision of a single-stranded DNA molecule (T-strand

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Gafni, Yedidya, and Vitaly Citovsky. Molecular interactions of TYLCV capsid protein during assembly of viral particles. United States Department of Agriculture, 2007. http://dx.doi.org/10.32747/2007.7587233.bard.

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Tomato yellow leaf curl geminivirus (TYLCV) is a major pathogen of cultivated tomato, causing up to 100% crop loss in many parts of the world. The present proposal, a continuation of a BARD-funded project, expanded our understanding of the molecular mechanisms by which CP molecules, as well as its pre-coat partner V2, interact with each other (CP), with the viral genome, and with cellular proteins during assembly and movement of the infectious virions. Specifically, two major objectives were proposed: I. To study in detail the molecular interactions between CP molecules and between CP and ssDN

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Czosnek, Henryk Hanokh, Dani Zamir, Robert L. Gilbertson, and Lucas J. William. Resistance to Tomato Yellow Leaf Curl Virus by Combining Expression of a Natural Tolerance Gene and a Dysfunctional Movement Protein in a Single Cultivar. United States Department of Agriculture, 2000. http://dx.doi.org/10.32747/2000.7573079.bard.

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Background The tomato yellow leaf curl disease (TYLCV) has been a major deterrent to tomato production in Israel for the last 20 years. This whitefly-transmitted viral disease has been found in the Caribbean Island in the early 1990s, probably as an import from the Middle East. In the late 1990s, the virus has spread to the US and is now conspicuous in Florida and Georgia. Objectives Because of the urgency facing the TYLCV epidemics, there was a compelling need to mobilize scientists to develop tomato variety resistant to TYLCV. The major goal was to identify the virus movement protein (MP) an

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Izhar, Shamay, Maureen Hanson, and Nurit Firon. Expression of the Mitochondrial Locus Associated with Cytoplasmic Male Sterility in Petunia. United States Department of Agriculture, 1996. http://dx.doi.org/10.32747/1996.7604933.bard.

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The main goal of the proposed research was to continue the mutual investigations into the molecular basis of CMS and male fertility restoration [MRF], with the ultimate goal of understanding these phenomena in higher plants. The experiments focused on: (1) dissecting apart the complex CMS - specific mitochondrial S-Pcf locus, in order to distinguish its essential parts which cause sterility from other parts and study its molecular evolution. (2) Studying the expression of the various regions of the S-Pcf locus in fertile and sterile lines and comparing the structure and ultrastructure of steri

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Sadot, Einat, Christopher Staiger, and Mohamad Abu-Abied. Studies of Novel Cytoskeletal Regulatory Proteins that are Involved in Abiotic Stress Signaling. United States Department of Agriculture, 2011. http://dx.doi.org/10.32747/2011.7592652.bard.

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In the original proposal we planned to focus on two proteins related to the actin cytoskeleton: TCH2, a touch-induced calmodulin-like protein which was found by us to interact with the IQ domain of myosin VIII, ATM1; and ERD10, a dehydrin which was found to associate with actin filaments. As reported previously, no other dehydrins were found to interact with actin filaments. In addition so far we were unsuccessful in confirming the interaction of TCH2 with myosin VIII using other methods. In addition, no other myosin light chain candidates were found in a yeast two hybrid survey. Nevertheless

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Alfano, James, Isaac Barash, Thomas Clemente, Paul E. Staswick, Guido Sessa, and Shulamit Manulis. Elucidating the Functions of Type III Effectors from Necrogenic and Tumorigenic Bacterial Pathogens. United States Department of Agriculture, 2010. http://dx.doi.org/10.32747/2010.7592638.bard.

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Many phytopathogenic bacteria use a type III protein secretion system (T3SS) to inject type III effectors into plant cells. In the experiments supported by this one-year feasibility study we investigated type III effector function in plants by using two contrasting bacterial pathogens: Pseudomonas syringae pv. tomato, a necrotrophic pathogen and Pantoea agglomerans, a tumorigenic pathogen. The objectives are listed below along with our major conclusions, achievements, and implications for science and agriculture. Objective 1: Compare Pseudomonas syringae and Pantoea agglomerans type III effect

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