1999
DOI: 10.1021/bi991675l
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The ‘KMSKS' Motif in Tyrosyl-tRNA Synthetase Participates in the Initial Binding of tRNATyr

Abstract: Variants at each position of the 'KMSKS' signature motif in tyrosyl-tRNA synthetase have been analyzed to test the hypothesis that this motif is involved in catalysis of the second step of the aminoacylation reaction (i.e., the transfer of tyrosine from the enzyme-bound tyrosyl-adenylate intermediate to the tRNA(Tyr) substrate). Pre-steady-state kinetic studies show that while the rate constants for tyrosine transfer (k(4)) are similar to the wild-type value for all of the mobile loop variants, the K230A and K… Show more

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Cited by 32 publications
(33 citation statements)
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“…This result is not unexpected since a characteristic feature of T. thermophilus PheRS is the highest affinity observed for synthetase-tRNA complexes at physiological pH. For a limited number of synthetases the dissociation constants of complexes with cognate tRNAs were found to be in the range 7-14 nM (Glasfeld et al, 1996;Ohannesian and Hou, 1996;Bullock et al, 2000), while most systems have K d values on the order of 0.1-1 mM (for reviews see Meinnel et al, 1995;Gale et al, 1996;Bovee et al, 1999;Ibba et al, 1999;Xin et al, 2000). Furthermore, some of the K d measurements have been performed at low pH, which may increase the binding affinity.…”
Section: Discussionmentioning
confidence: 87%
“…This result is not unexpected since a characteristic feature of T. thermophilus PheRS is the highest affinity observed for synthetase-tRNA complexes at physiological pH. For a limited number of synthetases the dissociation constants of complexes with cognate tRNAs were found to be in the range 7-14 nM (Glasfeld et al, 1996;Ohannesian and Hou, 1996;Bullock et al, 2000), while most systems have K d values on the order of 0.1-1 mM (for reviews see Meinnel et al, 1995;Gale et al, 1996;Bovee et al, 1999;Ibba et al, 1999;Xin et al, 2000). Furthermore, some of the K d measurements have been performed at low pH, which may increase the binding affinity.…”
Section: Discussionmentioning
confidence: 87%
“…Rate and dissociation constants are shown next to the steps to which they correspond. Values for the rate and dissociation constants are taken from [85] and [86]. .…”
Section: Discussionmentioning
confidence: 99%
“…The more conserved KMSKS sequence is located in a loop just downstream of the LS-domain. The role of the mobile KMSKS motif in the class I tryosyl-tRNA synthetase (TyrRS) has been extensively analyzed via structural and biochemical investigations at various stages of the reaction (33)(34)(35)(36). Upon ATP binding, the KMSKS loop shifts to a "closed" conformation where the two lysines interact with the α-and β-phosphates of the ATP molecule respectively, moving it closer to the active site (36).…”
Section: Discussionmentioning
confidence: 99%