Three-Dimensional Organization of the 30S Ribosomal Proteins from Escherichia coli, I. Preliminary Classification of the Proteins

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 protein...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 67; no. 3; pp. 1329 - 1336
Main Authors Craven, Gary R., Gupta, Vatsala
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 01.11.1970
National Acad Sciences
Subjects
Bacterial Proteins - classification
Biochemistry
Biological Sciences: Biochemistry
Centrifugation
Centrifugation, Density Gradient
Centrifugation, Zonal
Chromatography
Electrophoresis
Escherichia coli
Gels
Iodoacetates
Models, Biological
Nitrophenols - pharmacology
Reactivity
Reagents
Ribosomal proteins
Ribosomes
Trypsin - pharmacology
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.67.3.1329