Inactivation of Escherichia coli elongation factor Ts by the arginine-specific reagent butanedione.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)37728-1 ◽

1979 ◽

Vol 254 (6) ◽

pp. 1816-1820

Author(s):

A.H. MarSchel ◽

J.W. Bodley

Keyword(s):

Escherichia Coli ◽

Elongation Factor ◽

Specific Reagent

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Structure-function relationships in Escherichia coli translational elongation factor G: modification of lysine residues by the site-specific reagent pyridoxal phosphate

Biochemistry ◽

10.1021/bi00264a018 ◽

1982 ◽

Vol 21 (21) ◽

pp. 5224-5230 ◽

Author(s):

Alfonso Giovane ◽

Ciro Balestrieri ◽

Claudio Gualerzi

Keyword(s):

Escherichia Coli ◽

Structure Function ◽

Pyridoxal Phosphate ◽

Elongation Factor ◽

Elongation Factor G ◽

Site Specific ◽

Lysine Residues ◽

Specific Reagent ◽

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Inactivation of Escherichia coli elongation factor Tu by the arginine-specific reagent butanedione

Archives of Biochemistry and Biophysics ◽

10.1016/0003-9861(80)90206-4 ◽

1980 ◽

Vol 203 (2) ◽

pp. 489-495 ◽

Author(s):

Ardin H. Marschel ◽

James W. Bodley

Keyword(s):

Escherichia Coli ◽

Elongation Factor ◽

Elongation Factor Tu ◽

Specific Reagent

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Chemical modification in situ of Escherichia coli 50 S ribosomal proteins by the site-specific reagent pyridoxal phosphate. Inactivation of the elongation factor-G-dependent GTPase and of the association with the small ribosomal subunit.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)33234-4 ◽

1983 ◽

Vol 258 (1) ◽

pp. 157-162

Author(s):

H Ohsawa ◽

E Ohsawa ◽

A Giovane ◽

C Gualerzi

Keyword(s):

Escherichia Coli ◽

Chemical Modification ◽

Ribosomal Proteins ◽

Pyridoxal Phosphate ◽

Ribosomal Subunit ◽

Elongation Factor ◽

Small Ribosomal Subunit ◽

Site Specific ◽

Specific Reagent

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Chemical and physical studies on the structure of Escherichia coli elongation factor G.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)41006-5 ◽

1975 ◽

Vol 250 (17) ◽

pp. 6831-6836

Author(s):

M S Rohrbach ◽

J W Bodley ◽

K G Mann

Keyword(s):

Escherichia Coli ◽

Elongation Factor ◽

Elongation Factor G ◽

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Effect of trypsin modification of the Escherichia coli elongation factor Tu on the ternary complex with aminoacyl-tRNA.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)39406-1 ◽

1985 ◽

Vol 260 (15) ◽

pp. 8702-8705 ◽

Author(s):

E Masuda ◽

A Louie ◽

F Jurnak

Keyword(s):

Escherichia Coli ◽

Ternary Complex ◽

Elongation Factor ◽

Elongation Factor Tu

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The elongation factor Tu coded by the tufA gene of Escherichia coli K-12 is almost identical to that coded by the tufB gene.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)71878-4 ◽

1977 ◽

Vol 252 (6) ◽

pp. 2154-2157 ◽

Author(s):

A V Furano

Keyword(s):

Escherichia Coli ◽

Elongation Factor ◽

Elongation Factor Tu ◽

K 12 ◽

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Binding interactions between radiolabeled Escherichia coli elongation factor G and the ribosome.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)33719-5 ◽

1976 ◽

Vol 251 (6) ◽

pp. 1795-1798

Author(s):

L Lin ◽

J W Bodley

Keyword(s):

Escherichia Coli ◽

Elongation Factor ◽

Elongation Factor G ◽

Binding Interactions ◽

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Stimulation of Escherichia coli adenylate cyclase activity by elongation factor Tu, a GTP-binding protein essential for protein synthesis.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)67263-1 ◽

1986 ◽

Vol 261 (25) ◽

pp. 11448-11451

Author(s):

P Reddy ◽

D Miller ◽

A Peterkofsky

Keyword(s):

Escherichia Coli ◽

Protein Synthesis ◽

Adenylate Cyclase ◽

Elongation Factor ◽

Cyclase Activity ◽

Adenylate Cyclase Activity ◽

Elongation Factor Tu ◽

Gtp Binding Protein ◽

Gtp Binding ◽

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Biochemical and structural studies of the tetragonal crystalline modification of the Escherichia coli elongation factor Tu.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)43636-8 ◽

1980 ◽

Vol 255 (14) ◽

pp. 6751-6757

Author(s):

F. Jurnak ◽

A. McPherson ◽

A.H. Wang ◽

A. Rich

Keyword(s):

Escherichia Coli ◽

Elongation Factor ◽

Elongation Factor Tu ◽

Structural Studies ◽

Crystalline Modification

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Elongation factor G-dependent binding of a photoreactive GTP analogue to Escherichia coli ribosomes results in labeling of protein L11.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)40890-8 ◽

1978 ◽

Vol 253 (8) ◽

pp. 2777-2783 ◽

Author(s):

J.A. Maassen ◽

W. Möller

Keyword(s):

Escherichia Coli ◽

Elongation Factor ◽

Elongation Factor G ◽

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