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2. Topography of <em>Escherichia coli</em> Ribosomal Protein L12 <em>in situ</em>.

Author

Hasnain, Sadiq and Visentin, Louis Peter

Subjects
*PHYSICAL constants, *ENTEROBACTERIACEAE, *ESCHERICHIA coli, *HYDROGEN-ion concentration, *ESCHERICHIA, *XENORHABDUS
Abstract

The ionization constants of each individual free amino group of Escherichia coli ribosomal protein L12 as it exists on the native intact 50-S subunit has been determined. All these amino groups are exposed and have pK values varying from 9,7 to 11,0, The amino terminus, on the other hand, is unreactive and therefore appears to be buried. In addition, the reactivities indicate that the aminoterminal region of residues 1-59 undergoes a pH-dependent conformational change on the 50-S subunit. [ABSTRACT FROM AUTHOR]

Published
1977
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3. Ribosomal protein S1/S1A in bacteria

Author

Visentin, Louis Peter, Hasnain, Sadiq, Gallin, Warren, Johnson, Kenneth Glen, Griffith, Douglas W., and Wahba, Albert J.

Subjects
Halobacterium, Ribosomal Proteins, 5.8S ribosomal RNA, Biophysics, Biochemistry, 18S ribosomal RNA, Geobacillus stearothermophilus, 5S ribosomal RNA, Bacterial Proteins, Species Specificity, Structural Biology, Ribosomal protein, 28S ribosomal RNA, Escherichia coli, Genetics, Amino Acid Sequence, Amino Acids, Arthrobacter, Molecular Biology, 50S, Antigens, Bacterial, Eukaryotic Large Ribosomal Subunit, Chemistry, Cell Biology, Ribosomal RNA, Molecular Weight
Published
1977

7. Procaryotic Ribosomal Proteins: N-Terminal Sequence Homologies and Structural Correspondence of 30 S Ribosomal Proteins from Escherichia coli and Bacillus stearothermophilus

Author

NATIONAL RESEARCH COUNCIL OF CANADA OTTAWA (ONTARIO) DIV OF BIOLOGICAL SCIENCES, Yaguchi,Makoto, Matheson,Alastair Taylor, Visentin,Louis Peter, NATIONAL RESEARCH COUNCIL OF CANADA OTTAWA (ONTARIO) DIV OF BIOLOGICAL SCIENCES, Yaguchi,Makoto, Matheson,Alastair Taylor, and Visentin,Louis Peter

Abstract

In attempting to evidence the evolution and the structure--function relationships of the ribosome in procaryotes the authors have undertaken a comparative amino acid sequence analysis of ribosomal proteins from Escherichia coli, and Bacillus stearothermophilus and Halobacterium cutirubrum, organisms which differ substantially in their physiological tolerances and taxonomic relationships. Previous structural studies have indicated a high degree of homology in some of the 30 S ribosomal proteins from E. coli and B. stearothermophilus. Reported in this paper is a summary of results on the study of the amino terminal regions of 19 ribosomal proteins E. coli strain Q13 and 21 from B. stearothermophilus strain 10.

Published
1974

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