Conformational changes in ribosomes upon interaction with elongation factors

Biochimie
A T Gudkov, M G Bubunenko

Abstract

Conformational changes in the ribosomes upon interaction with EF-Tu were studied by limited proteolysis with a set of proteases. The main results are: (1) The cleavage rate of S1 protein strongly depends on the cooperative effect of poly(U) and tRNA: (2) The conformation of L7/L12 proteins is modulated by interaction of elongation factors with the ribosome and depends on hydrolysis of GTP; (3) The sensitivity of some ribosomal proteins (S6, S7, S18, S19, L9, L16, L19, and L27) to proteases changes upon binding of EF-Tu and depends on the ribosome functional state in accordance with GTP hydrolysis. Most of these proteins are located far from the factor-binding center of the ribosome. The possible mechanism of conformational changes is discussed.

Citations

Jul 1, 1991·Biochimie·W Möller
May 1, 1992·Biochimie·M G BubunenkoA T Gudkov
Mar 21, 2002·FEBS Letters·Alexander S Spirin
Mar 7, 1997·The Journal of Biological Chemistry·R Kambampati, K Chakraburtty
Nov 1, 1995·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·A LiljasE Brazhnikov
Apr 9, 2005·The Journal of Biological Chemistry·Matthew W VettingJohn S Blanchard
Apr 5, 2000·The Journal of Biological Chemistry·R KambampatiK Chakraburtty
Feb 13, 2004·The Journal of Biological Chemistry·Eduard V BocharovAlexander S Arseniev
Mar 1, 1996·Microbiological Reviews·G Caponigro, R Parker

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