Выключение синтеза белка в бактериальной клетке с помощью олигоглутамилирования рибосомного белка S6 (1105555), страница 17
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B. Kade, E.R. Dabbs, B. Wittmann-Liebold. Protein-chemical studies on Escherichia colimutants with altered ribosomal proteins S6 and S7. // FEBS Letters. 1980. V. 121. P.313-316.78. M. Kitakawa, L. Blumenthal, K. Isono. Isolation and characterization of specializedtransducing lambda phages carrying ribosomal protein genes of Escherichia coli. // MolGen Genet. 1980.
V. 180. P. 343-349.79. E.V. Koonin, P. Bork, C. Sander. A novel RNA-binding motif in omnipotent suppressors oftranslation termination, ribosomal proteins and a ribosome modification enzyme? //Nucleic Acids Res. 1994. V. 22. P. 2166-2167.80.
M.Y. Galperin, E.V. Koonin. A diverse superfamily of enzymes with ATP-dependentcarboxylate-amine/thiol ligase activity. // Protein Sci. 1997. V. 6. P. 2639-2643.81. K. Kino, T. Arai, Y. Arimura. Poly-alpha-glutamic acid synthesis using a novel catalyticactivity of RimK from Escherichia coli K-12. // Appl Environ Microbiol. 2011.
V. 77. P.2019-2025.82. G. Zhao, Z. Jin, Y. Wang, N.M. Allewell, M. Tuchman, D. Shi. Structure and function ofEscherichia coli RimK, an ATP-grasp fold, L-glutamyl ligase enzyme. // Proteins. 2013.V. 81. P. 1847-1854.83. I.A. Osterman, A.V. Ustinov, D.V.
Evdokimov, V.A. Korshun, P.V. Sergiev, M.V.Serebryakova, I.A. Demina, M.A. Galyamina, V.M. Govorun, O.A. Dontsova. A nascentproteome study combining click chemistry with 2DE. // Proteomics. 2013. V. 13. P. 1721.84. A.L. Starosta, J. Lassak, K. Jung, D.N. Wilson. The bacterial translation stress response. //FEMS Microbiol Rev. 2014.85. Y.S. Polikanov, G.M. Blaha, T.A. Steitz. How hibernation factors RMF, HPF, and YfiA turnoff protein synthesis. // Science. 2012.
V. 336. P. 915-918.86. H. Yoshida, A. Wada. The 100S ribosome: ribosomal hibernation induced by stress. // WileyInterdiscip Rev RNA. 2014. V. 5. P. 723-732.10687. T. Kato, H. Yoshida, T. Miyata, Y. Maki, A. Wada, K. Namba. Structure of the 100Sribosome in the hibernation stage revealed by electron cryomicroscopy. // Structure.2010. V. 18. P. 719-724.88. R. Hauser, M. Pech, J. Kijek, H.
Yamamoto, B. Titz, F. Naeve, A. Tovchigrechko, K.Yamamoto, W. Szaflarski, N. Takeuchi, T. Stellberger, M.E. Diefenbacher, K.H.Nierhaus, P. Uetz. RsfA (YbeB) proteins are conserved ribosomal silencing factors. //PLoS Genet. 2012. V. 8. P. e1002815.89. G. Boel, P.C. Smith, W. Ning, M.T. Englander, B. Chen, Y. Hashem, A.J. Testa, J.J. Fischer,H.J. Wieden, J. Frank, R.L. Gonzalez, Jr., J.F. Hunt.
The ABC-F protein EttA gatesribosome entry into the translation elongation cycle. // Nat Struct Mol Biol. 2014. V. 21.P. 143-151.90. B. Chen, G. Boel, Y. Hashem, W. Ning, J. Fei, C. Wang, R.L. Gonzalez, Jr., J.F. Hunt, J.Frank. EttA regulates translation by binding the ribosomal E site and restrictingribosome-tRNA dynamics. // Nat Struct Mol Biol. 2014. V. 21. P.
152-159.91. H. Yoshida, Y. Maki, S. Furuike, A. Sakai, M. Ueta, A. Wada. YqjD is an inner membraneprotein associated with stationary-phase ribosomes in Escherichia coli. // J Bacteriol.2012. V. 194. P. 4178-4183.92. K. Izutsu, C. Wada, Y. Komine, T. Sako, C. Ueguchi, S. Nakura, A.
Wada. Escherichia coliribosome-associated protein SRA, whose copy number increases during stationary phase.// J Bacteriol. 2001. V. 183. P. 2765-2773.93. S.E. Finkel. Long-term survival during stationary phase: evolution and the GASP phenotype.// Nat Rev Microbiol. 2006. V. 4.
P. 113-120.94. K. Lewis. Persister cells, dormancy and infectious disease. // Nat Rev Microbiol. 2007. V. 5.P. 48-56.95. E. Germain, D. Castro-Roa, N. Zenkin, K. Gerdes. Molecular mechanism of bacterialpersistence by HipA. // Mol Cell. 2013. V.
52. P. 248-254.96. I. Ruvinsky, O. Meyuhas. Ribosomal protein S6 phosphorylation: from protein synthesis tocell size. // Trends Biochem Sci. 2006. V. 31. P. 342-348.97. K.A. Datsenko, B.L. Wanner. One-step inactivation of chromosomal genes in Escherichiacoli K-12 using PCR products. // Proc Natl Acad Sci U S A. 2000. V. 97. P. 6640-6645.98. T. Baba, T. Ara, M.
Hasegawa, Y. Takai, Y. Okumura, M. Baba, K.A. Datsenko, M. Tomita,B.L. Wanner, H. Mori. Construction of Escherichia coli K-12 in-frame, single-geneknockout mutants: the Keio collection. // Mol Syst Biol. 2006. V. 2. P. 2006 0008.99. M. Kitagawa, T. Ara, M. Arifuzzaman, T. Ioka-Nakamichi, E. Inamoto, H. Toyonaga, H.Mori. Complete set of ORF clones of Escherichia coli ASKA library (a complete set of107E. coli K-12 ORF archive): unique resources for biological research. // DNA Res. 2005.V.
12. P. 291-299.100. F.V. Subach, O.M. Subach, I.S. Gundorov, K.S. Morozova, K.D. Piatkevich, A.M. Cuervo,V.V. Verkhusha. Monomeric fluorescent timers that change color from blue to red reporton cellular trafficking. // Nat Chem Biol. 2009. V. 5. P. 118-126.101. J. Sambrook, D.W. Russel, Molecular Cloning: A Laboratory Manual, Cold Spring HarborLaboratory Press, 2001.102.
H. Inoue, H. Nojima, H. Okayama. High efficiency transformation of Escherichia coli withplasmids. // Gene. 1990. V. 96. P. 23-28.103. K.H. Nierhaus, Reconstitution of ribosomes, in: G. Spedding (Ed.), Ribosomes and proteinsynthesis: a practical approach., IRL Press, Oxford, 1990, pp. 161-189.104. M.M. Bradford. A rapid and sensitive method for the quantitation of microgram quantitiesof protein utilizing the principle of protein-dye binding. // Anal Biochem. 1976. V.
72. P.248-254.105. M.S. Svetlov, A. Kommer, V.A. Kolb, A.S. Spirin. Effective cotranslational folding offirefly luciferase without chaperones of the Hsp70 family. // Protein Sci. 2006. V. 15. P.242-247.108.