PMID- 6816267
OWN - NLM
STAT- MEDLINE
DCOM- 19830214
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 21
IP  - 21
DP  - 1982 Oct 12
TI  - Structure-function relationships in Escherichia coli translational elongation 
      factor G: modification of lysine residues by the site-specific reagent pyridoxal 
      phosphate.
PG  - 5224-30
AB  - Translational elongation factor G (EF-G) of Escherichia coli was modified with 
      the selective, site-specific lysine reagent pyridoxal phosphate (PLP). The 
      reaction results in the modification of a maximum of 12 lysine residues, one of 
      which is essential for guanosine 5'-triphosphate (GTP) binding and whose 
      modification is inhibited by the presence of GTP. Formation of a reversible 
      adduct between 2,3-butanedione and an essential arginine similarly located in the 
      GTP binding site [Rohrbach, M.S., & Bodley, J. W. (1977) Biochemistry 16, 
      1360-1363] also protects EF-G from PLP inactivation, suggesting that these two 
      residues are spatially close to each other in the native factor. The essential 
      lysine residue was found in the trypsin-resistant fragment T4 (Mr 41 000). In 
      addition to the lysine essential for GTP binding, at least one further lysine was 
      found to be important for EF-G function, since GTP-protected, PLP-modified EF-G 
      molecules fully competent in binding to 50S ribosomal subunits showed decreased 
      activity in 50S- and 70S-dependent GTP hydrolysis. It is likely that a 
      PLP-modified lysine impairs the interaction of the factor with 30S ribosomal 
      subunits and/or a conformational change of the factor required for the hydrolysis 
      of GTP.
FAU - Giovane, A
AU  - Giovane A
FAU - Balestrieri, C
AU  - Balestrieri C
FAU - Gualerzi, C
AU  - Gualerzi C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Peptide Elongation Factor G)
RN  - 0 (Peptide Elongation Factors)
RN  - 5V5IOJ8338 (Pyridoxal Phosphate)
RN  - EC 3.4.21.4 (Trypsin)
RN  - K3Z4F929H6 (Lysine)
SB  - IM
MH  - Escherichia coli/*analysis
MH  - Lysine/*metabolism
MH  - Mathematics
MH  - Peptide Elongation Factor G
MH  - Peptide Elongation Factors/*metabolism
MH  - Protein Biosynthesis
MH  - Pyridoxal Phosphate/*metabolism
MH  - Structure-Activity Relationship
MH  - Time Factors
MH  - Trypsin/metabolism
EDAT- 1982/10/12 00:00
MHDA- 1982/10/12 00:01
CRDT- 1982/10/12 00:00
PHST- 1982/10/12 00:00 [pubmed]
PHST- 1982/10/12 00:01 [medline]
PHST- 1982/10/12 00:00 [entrez]
AID - 10.1021/bi00264a018 [doi]
PST - ppublish
SO  - Biochemistry. 1982 Oct 12;21(21):5224-30. doi: 10.1021/bi00264a018.