Elongation factors Tu and G change their conformation on interaction with ribosomes.
Limited trypsinolysis was used to study conformational changes in elongation factors Tu and G. The trypsin cleavage rates of the factors differed and depended on both their interaction with ligands and the presence or absence of ribosomes. When the factors were bound to ribosomes, changes in their sensitivity to trypsin were observed depending on whether GDP or GTP was present in the complex, i.e. on the hydrolysis state of the guanine nucleotide ligand. The possible significance of factor structural changes for their functioning is discussed.
Bubunenko
M G
MG
Institute of Protein Research, Academy of Sciences of the USSR, Pushchino, Moscow Region.
Gudkov
A T
AT
D004591:Electrophoresis, Polyacrylamide Gel; D006160:Guanosine Triphosphate / Q000378:metabolism; D008024:Ligands; D020653:Peptide Elongation Factor G; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000378:metabolism; D010445:Peptide Elongation Factors / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D012270:Ribosomes / Q000378:metabolism*; D014357:Trypsin
D008024:Ligands; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D006160:Guanosine Triphosphate; D014357:Trypsin; D010444:Peptide Elongation Factor Tu