RNA binding properties of the coat protein from bacteriophage GA

Jonatha M. Gott; Larry J. Wilhelm; C. Uhlenbeck Olke

doi:10.1093/nar/19.23.6499

RNA binding properties of the coat protein from bacteriophage GA

Jonatha M. Gott, Larry J. Wilhelm, C. Uhlenbeck Olke^*

^*Corresponding author for this work

Molecular Biosciences

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

26 Scopus citations

Abstract

The coat protein of bacteriophage GA, a group II RNA phage, binds to a small RNA hairpin corresponding to its replicase operator. Binding is specific, with a Ka of 71 μM^-1 This interaction differs kinetically from the analogous coat protein-RNA hairpin interactions of other RNA phage and also deviates somewhat in its pH and salt dependence. Despite 46 of 129 amino acid differences between the GA and group I phage R17 coat proteins, the binding sites are fairly similar. The essential features of the GA coat protein binding site are a based-paired stem with an unpaired purine and a four nucleotide loop having an A at position -4 and a purine at -7 . Unlike the group I phage proteins, the GA coat protein does not distinguish between two alternate positions for the unpaired purine and does not show high specificity for a pyrimidine at position -5 of the loop.

Original language	English (US)
Pages (from-to)	6499-6503
Number of pages	5
Journal	Nucleic acids research
Volume	19
Issue number	23
DOIs	https://doi.org/10.1093/nar/19.23.6499
State	Published - Dec 11 1991

ASJC Scopus subject areas

Genetics

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title = "RNA binding properties of the coat protein from bacteriophage GA",

abstract = "The coat protein of bacteriophage GA, a group II RNA phage, binds to a small RNA hairpin corresponding to its replicase operator. Binding is specific, with a Ka of 71 μM-1 This interaction differs kinetically from the analogous coat protein-RNA hairpin interactions of other RNA phage and also deviates somewhat in its pH and salt dependence. Despite 46 of 129 amino acid differences between the GA and group I phage R17 coat proteins, the binding sites are fairly similar. The essential features of the GA coat protein binding site are a based-paired stem with an unpaired purine and a four nucleotide loop having an A at position -4 and a purine at -7 . Unlike the group I phage proteins, the GA coat protein does not distinguish between two alternate positions for the unpaired purine and does not show high specificity for a pyrimidine at position -5 of the loop.",

author = "Gott, {Jonatha M.} and Wilhelm, {Larry J.} and Olke, {C. Uhlenbeck}",

note = "Funding Information: The authors are grateful to Dr. Lars Liljas for providing the MS2 crystal structure coordinates and to Dr. Gary Witherell for helpful discussions. This work was supported by a National Institutes of Health Postdoctoral Fellowship Grant (GM-12452) to J. M. G. and by a National Institutes of Health Grant (GM-36944) to O. C. U. We also thank the W. M. Keck Foundation for their generous support of RNA science on the Boulder Campus.",

year = "1991",

month = dec,

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doi = "10.1093/nar/19.23.6499",

language = "English (US)",

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AU - Gott, Jonatha M.

AU - Wilhelm, Larry J.

AU - Olke, C. Uhlenbeck

N1 - Funding Information: The authors are grateful to Dr. Lars Liljas for providing the MS2 crystal structure coordinates and to Dr. Gary Witherell for helpful discussions. This work was supported by a National Institutes of Health Postdoctoral Fellowship Grant (GM-12452) to J. M. G. and by a National Institutes of Health Grant (GM-36944) to O. C. U. We also thank the W. M. Keck Foundation for their generous support of RNA science on the Boulder Campus.

PY - 1991/12/11

Y1 - 1991/12/11

N2 - The coat protein of bacteriophage GA, a group II RNA phage, binds to a small RNA hairpin corresponding to its replicase operator. Binding is specific, with a Ka of 71 μM-1 This interaction differs kinetically from the analogous coat protein-RNA hairpin interactions of other RNA phage and also deviates somewhat in its pH and salt dependence. Despite 46 of 129 amino acid differences between the GA and group I phage R17 coat proteins, the binding sites are fairly similar. The essential features of the GA coat protein binding site are a based-paired stem with an unpaired purine and a four nucleotide loop having an A at position -4 and a purine at -7 . Unlike the group I phage proteins, the GA coat protein does not distinguish between two alternate positions for the unpaired purine and does not show high specificity for a pyrimidine at position -5 of the loop.

AB - The coat protein of bacteriophage GA, a group II RNA phage, binds to a small RNA hairpin corresponding to its replicase operator. Binding is specific, with a Ka of 71 μM-1 This interaction differs kinetically from the analogous coat protein-RNA hairpin interactions of other RNA phage and also deviates somewhat in its pH and salt dependence. Despite 46 of 129 amino acid differences between the GA and group I phage R17 coat proteins, the binding sites are fairly similar. The essential features of the GA coat protein binding site are a based-paired stem with an unpaired purine and a four nucleotide loop having an A at position -4 and a purine at -7 . Unlike the group I phage proteins, the GA coat protein does not distinguish between two alternate positions for the unpaired purine and does not show high specificity for a pyrimidine at position -5 of the loop.

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RNA binding properties of the coat protein from bacteriophage GA

Abstract

ASJC Scopus subject areas

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