Proximity of 5.8 S RNA-binding proteins and A-site proteins in yeast ribosomes inferred from cross-linking

J. C. Lee; R. R. Traut

Proximity of 5.8 S RNA-binding proteins and A-site proteins in yeast ribosomes inferred from cross-linking

J. C. Lee, R. R. Traut

Biochemistry & Structural Biology

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

6 Scopus citations

Abstract

In order to probe the spatial arrangement of proteins within the 5.8 S rRNA domain of the intact ribosomal subunit of Saccharomyces cerevisiae, 60 S ribosomal subunits were treated with 2-iminothiolane. Proteins were extracted from the cross-linked ribosomes, fractionated by Sephadex G-150 column chromatography, and analyzed by diagonal polyacrylamide-sodium dodecyl sulfate gel electrophoresis. Constituent proteins of cross-linked pairs were identified by two-dimensional polyacrylamide gel electrophoresis. Nine cross-links involving five of the 11 5.8 S rRNA-binding proteins were analyzed. A model showing the network of cross-links is presented. Several of the 5.8 S rRNA-binding proteins are in sufficiently close proximity of the ribosomal A-site proteins to be cross-linked.

Original language	English (US)
Pages (from-to)	9971-9974
Number of pages	4
Journal	Journal of Biological Chemistry
Volume	259
Issue number	16
State	Published - Jan 1 1984

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "Proximity of 5.8 S RNA-binding proteins and A-site proteins in yeast ribosomes inferred from cross-linking",

abstract = "In order to probe the spatial arrangement of proteins within the 5.8 S rRNA domain of the intact ribosomal subunit of Saccharomyces cerevisiae, 60 S ribosomal subunits were treated with 2-iminothiolane. Proteins were extracted from the cross-linked ribosomes, fractionated by Sephadex G-150 column chromatography, and analyzed by diagonal polyacrylamide-sodium dodecyl sulfate gel electrophoresis. Constituent proteins of cross-linked pairs were identified by two-dimensional polyacrylamide gel electrophoresis. Nine cross-links involving five of the 11 5.8 S rRNA-binding proteins were analyzed. A model showing the network of cross-links is presented. Several of the 5.8 S rRNA-binding proteins are in sufficiently close proximity of the ribosomal A-site proteins to be cross-linked.",

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year = "1984",

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T1 - Proximity of 5.8 S RNA-binding proteins and A-site proteins in yeast ribosomes inferred from cross-linking

AU - Lee, J. C.

AU - Traut, R. R.

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N2 - In order to probe the spatial arrangement of proteins within the 5.8 S rRNA domain of the intact ribosomal subunit of Saccharomyces cerevisiae, 60 S ribosomal subunits were treated with 2-iminothiolane. Proteins were extracted from the cross-linked ribosomes, fractionated by Sephadex G-150 column chromatography, and analyzed by diagonal polyacrylamide-sodium dodecyl sulfate gel electrophoresis. Constituent proteins of cross-linked pairs were identified by two-dimensional polyacrylamide gel electrophoresis. Nine cross-links involving five of the 11 5.8 S rRNA-binding proteins were analyzed. A model showing the network of cross-links is presented. Several of the 5.8 S rRNA-binding proteins are in sufficiently close proximity of the ribosomal A-site proteins to be cross-linked.

AB - In order to probe the spatial arrangement of proteins within the 5.8 S rRNA domain of the intact ribosomal subunit of Saccharomyces cerevisiae, 60 S ribosomal subunits were treated with 2-iminothiolane. Proteins were extracted from the cross-linked ribosomes, fractionated by Sephadex G-150 column chromatography, and analyzed by diagonal polyacrylamide-sodium dodecyl sulfate gel electrophoresis. Constituent proteins of cross-linked pairs were identified by two-dimensional polyacrylamide gel electrophoresis. Nine cross-links involving five of the 11 5.8 S rRNA-binding proteins were analyzed. A model showing the network of cross-links is presented. Several of the 5.8 S rRNA-binding proteins are in sufficiently close proximity of the ribosomal A-site proteins to be cross-linked.

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