Three-dimensional organization of the 30S ribosomal proteins from Escherichia coli. I. Preliminary classification of the proteins.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 67 ·No. 3 ·1970-11-00 ·Pages 1329-36

Craven GR, Gupta V

Abstract

30S ribosomal subunits from Escherichia coli were reacted with three protein reagents. After reaction, the ribosomal proteins were extracted and examined; of the 20 proteins known to compose the particle, nine did not react with any of the three reagents. We have tentatively classified these proteins as "internal," and the remaining eleven as "external." A strong correlation was found between these results and the sequence of assembly. Those proteins which enter the assembly process early are classed as internal, whereas those proteins found to participate later in the assembly sequence are classed as external.

MeSH Terms

Bacterial Proteins/classification Centrifugation, Density Gradient Centrifugation, Zonal Chromatography Electrophoresis Escherichia coli Iodoacetates Models, Biological Nitrophenols/pharmacology Ribosomes Trypsin/pharmacology

Chemicals

Bacterial Proteins Iodoacetates Nitrophenols Trypsin

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Craven G R

Gupta V

References (14)

14 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.67.3.1329

Published

1970-11-00

Pages

1329-36

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC283356

Subset

External Links

PubMed source DOI: 10.1073/pnas.67.3.1329 PMC Full Text View journal details

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Three-dimensional organization of the 30S ribosomal proteins from Escherichia coli. I. Preliminary classification of the proteins.

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