title: Conformational changes in ribosomes upon interaction with elongation factors.
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.
authors.affiliation: Institute of Protein Research, Academy of Sciences of the USSR, Moscow Region.
authors.forename: A T
authors.initials: AT
authors.lastname: Gudkov
authors.forename: M G
authors.initials: MG
authors.lastname: Bubunenko
mesh_terms: D004586:Electrophoresis; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D010444:Peptide Elongation Factor Tu / Q000502:physiology; D010447:Peptide Hydrolases / Q000378:metabolism; D011072:Poly U / Q000378:metabolism; D011487:Protein Conformation; D012343:RNA, Transfer / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism* / Q000648:ultrastructure; D014357:Trypsin / Q000378:metabolism
chemical_list: D012269:Ribosomal Proteins; C015494:ribosomal protein S1; D011072:Poly U; D006160:Guanosine Triphosphate; D012343:RNA, Transfer; D010447:Peptide Hydrolases; D014357:Trypsin; D010444:Peptide Elongation Factor Tu