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Science 27 March 1987:
Vol. 235. no. 4796, pp. 1651 - 1653
DOI: 10.1126/science.2435005
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Articles

Science, Vol 235, Issue 4796, 1651-1653
Copyright © 1987 by American Association for the Advancement of Science

articles

Polypeptide sequences essential for RNA recognition by an enzyme

L Regan, J Bowie, and P Schimmel

Many RNAs are complex, globular molecules formed from elements of secondary and tertiary structure analogous to those found in proteins. Little is known about recognition of RNAs by proteins. In the case of transfer RNAs (tRNAs), considerable evidence suggests that elements dispersed in both the one- and three-dimensional structure are important for recognition by aminoacyl tRNA synthetases. Fragments of alanine tRNA synthetase were created by in vitro manipulations of the cloned alaS gene and examined for their interaction with alanine-specific tRNA. Sequences essential for recognition were located near the middle of the polypeptide, juxtaposed to the carboxyl-terminal side of the domain for aminoacyl adenylate synthesis. The most essential part of the tRNA interaction strength and specificity was dependent on a sequence of fewer than 100 amino acids. Within this sequence, and in the context of the proper conformation, a segment of no more than 17 amino acids was responsible for 25% or more of the total synthetase-tRNA free energy of association. The results raise the possibility that an important part of specific RNA recognition by an aminoacyl tRNA synthetase involves a polypeptide segment that is short relative to the total size of the protein.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Natural Homolog of tRNA Synthetase Editing Domain Rescues Conditional Lethality Caused by Mistranslation.
Y. E. Chong, X.-L. Yang, and P. Schimmel (2008)
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Molecular basis of alanine discrimination in editing site.
M. Sokabe, A. Okada, M. Yao, T. Nakashima, and I. Tanaka (2005)
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Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase.
M. A. Swairjo and P. R. Schimmel (2005)
PNAS 102, 988-993
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Assembly of a catalytic unit for RNA microhelix aminoacylation using nonspecific RNA binding domains.
J. W. Chihade and P. Schimmel (1999)
PNAS 96, 12316-12321
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Changing the identity of a tRNA by introducing a G-U wobble pair near the 3' acceptor end.
W. McClain and K Foss (1988)
Science 240, 793-796
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Evidence for dispensable sequences inserted into a nucleotide fold.
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Science 237, 1614-1618
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Characterization by tandem mass spectrometry of structural modifications in proteins.
K Biemann and H. Scoble (1987)
Science 237, 992-998
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