Binding of yeast tRNAphe anticodon arm to Escherichia coli 30 S ribosomes

Samuel J. Rose; Peggy T. Lowary; Olke C. Uhlenbeck

doi:10.1016/S0022-2836(83)80036-9

Binding of yeast tRNA^phe anticodon arm to Escherichia coli 30 S ribosomes

Samuel J. Rose^*, Peggy T. Lowary, Olke C. Uhlenbeck

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

52 Scopus citations

Abstract

A 15-nucleotide fragment of RNA having the sequence of the anticodon arm of yeast tRNA^Phe was constructed using T4 RNA ligase. The stoichiometry and binding constant of this oligomer to poly(U)-programmed 30 S ribosomes was found to be identical to that of deacylated tRNA^Phe. The anticodon arm and tRNA^Phe also compete for the same binding site on the ribosome. These data indicate that the interaction of tRNA^Phe with poly(U)-programmed 30 S ribosomes is primarily a result of contacts in the anticodon arm region and not with other parts of the transfer RNA. Since similar oligomers which cannot form a stable helical stem do not bind ribosomes, a clear requirement for the entire anticodon arm structure is demonstrated.

Original language	English (US)
Pages (from-to)	103-117
Number of pages	15
Journal	Journal of Molecular Biology
Volume	167
Issue number	1
DOIs	https://doi.org/10.1016/S0022-2836(83)80036-9
State	Published - Jun 15 1983

Funding

This work was supported by a grant from the National Institutes of Health (GM19059).

ASJC Scopus subject areas

Biophysics
Structural Biology
Molecular Biology

Access to Document

10.1016/S0022-2836(83)80036-9

Cite this

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title = "Binding of yeast tRNAphe anticodon arm to Escherichia coli 30 S ribosomes",

abstract = "A 15-nucleotide fragment of RNA having the sequence of the anticodon arm of yeast tRNAPhe was constructed using T4 RNA ligase. The stoichiometry and binding constant of this oligomer to poly(U)-programmed 30 S ribosomes was found to be identical to that of deacylated tRNAPhe. The anticodon arm and tRNAPhe also compete for the same binding site on the ribosome. These data indicate that the interaction of tRNAPhe with poly(U)-programmed 30 S ribosomes is primarily a result of contacts in the anticodon arm region and not with other parts of the transfer RNA. Since similar oligomers which cannot form a stable helical stem do not bind ribosomes, a clear requirement for the entire anticodon arm structure is demonstrated.",

author = "Rose, {Samuel J.} and Lowary, {Peggy T.} and Uhlenbeck, {Olke C.}",

note = "Funding Information: This work was supported by a grant from the National Institutes of Health (GM19059).",

year = "1983",

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T1 - Binding of yeast tRNAphe anticodon arm to Escherichia coli 30 S ribosomes

AU - Rose, Samuel J.

AU - Lowary, Peggy T.

AU - Uhlenbeck, Olke C.

N1 - Funding Information: This work was supported by a grant from the National Institutes of Health (GM19059).

PY - 1983/6/15

Y1 - 1983/6/15

N2 - A 15-nucleotide fragment of RNA having the sequence of the anticodon arm of yeast tRNAPhe was constructed using T4 RNA ligase. The stoichiometry and binding constant of this oligomer to poly(U)-programmed 30 S ribosomes was found to be identical to that of deacylated tRNAPhe. The anticodon arm and tRNAPhe also compete for the same binding site on the ribosome. These data indicate that the interaction of tRNAPhe with poly(U)-programmed 30 S ribosomes is primarily a result of contacts in the anticodon arm region and not with other parts of the transfer RNA. Since similar oligomers which cannot form a stable helical stem do not bind ribosomes, a clear requirement for the entire anticodon arm structure is demonstrated.

AB - A 15-nucleotide fragment of RNA having the sequence of the anticodon arm of yeast tRNAPhe was constructed using T4 RNA ligase. The stoichiometry and binding constant of this oligomer to poly(U)-programmed 30 S ribosomes was found to be identical to that of deacylated tRNAPhe. The anticodon arm and tRNAPhe also compete for the same binding site on the ribosome. These data indicate that the interaction of tRNAPhe with poly(U)-programmed 30 S ribosomes is primarily a result of contacts in the anticodon arm region and not with other parts of the transfer RNA. Since similar oligomers which cannot form a stable helical stem do not bind ribosomes, a clear requirement for the entire anticodon arm structure is demonstrated.

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