Inactivation of Escherichia coli elongation factor Ts by the arginine-specific reagent butanedione.
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منابع مشابه
Inactivation of Escherichia coli elongation factor Tu by the arginine-specific reagent butanedione.
Elongation factor T, (EF-T,) is inactivated by the arginine-specific reagent 2,3-butanedione. Excess elongation factor T, (EF-T,), the protein substrate for EFT,, protects EF-T, from this inactivation. Borate ion affects the inactivation kinetics in a manner consistent with the formation of an arginine residueebutanedione l borate complex. The butanedione inactivation is rapidly reversible in t...
متن کاملInactivation of Escherichia coli Elongation Factor T, by the Arginine- specific Reagent Butanedione*
Elongation factor T, (EF-T,) is inactivated by the arginine-specific reagent 2,3-butanedione. Excess elongation factor T, (EF-T,), the protein substrate for EFT,, protects EF-T, from this inactivation. Borate ion affects the inactivation kinetics in a manner consistent with the formation of an arginine residueebutanedione l borate complex. The butanedione inactivation is rapidly reversible in t...
متن کاملThe identification of a domain in Escherichia coli elongation factor Tu that interacts with elongation factor Ts.
A method has been developed to search for the elongation factor Tu (EF-Tu) domain(s) that interact with elongation factor Ts (EF-Ts). This method is based on the suppression of Escherichia coli EF-Tu-dominant negative mutation K136E, a mutation that exerts its effect by sequestering EF-Ts. We have identified nine single-amino acid- substituted suppression mutations in the region 146-199 of EF-T...
متن کاملInactivation of Escherichia coli L-threonine dehydrogenase by 2,3-butanedione. Evidence for a catalytically essential arginine residue.
Incubation of homogeneous preparations of L-threonine dehydrogenase from Escherichia coli with 2,3-butanedione, 2,3-pentanedione, phenylglyoxal, or 1,2-cyclohexanedione causes a time- and concentration-dependent loss of enzymatic activity; plots of log percent activity remaining versus time are linear to greater than 90% inactivation, indicative of pseudo-first order inactivation kinetics. The ...
متن کاملRole of domains in Escherichia coli and mammalian mitochondrial elongation factor Ts in the interaction with elongation factor Tu.
Bovine mitochondrial elongation factor Ts (EF-Tsmt) stimulates the activity of Escherichia coli elongation factor Tu (EF-Tu). In contrast, E. coli EF-Ts is unable to stimulate mitochondrial EF-Tu. EF-Tsmt forms a tight complex with E. coli EF-Tu governed by an association constant of 8.6 x 10(10). This value is 100-fold stronger than the binding constant for the formation of the E. coli EF-Tu.T...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)37728-1