PMID:2657655: Difference between revisions
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!align=left |Citation | |||
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'''Bruckner, RC and Cox, MM''' (1989) The histone-like H protein of Escherichia coli is ribosomal protein S3. ''Nucleic Acids Res.'' '''17''':3145-61 | |||
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!align=left |Abstract | |||
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We report the purification of four proteins from Escherichia coli that stimulate or inhibit inter- and/or intramolecular recombination promoted by the yeast plasmid-encoded FLP protein. The proteins are identified as the ribosomal proteins S3 (27 kDa), L2 (26 kDa), S4 (24 kDa), and S5 (16 kDa), on the basis of N-terminal sequence analysis. The S3 protein is found to be identical to H protein, an E. coli histone-like protein that is related to histone H2A immunologically and by virtue of amino acid content. The H protein/S3 identity is based on co-migration on polyacrylamide gels, heat stability, amino acid analysis, and effects on FLP-promoted recombination. These results are relevant to current studies on the structure of the E. coli nucleoid. Since the H protein has previously been found associated with the E. coli nucleoid, the results indicate that either (a) some ribosomal proteins serve a dual function in E. coli, or, more likely, (b) ribosomal proteins can and are being mis-identified as nucleoid constituents. | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2657655 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC317720 PMC317720] | |||
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| | !align=left |Keywords | ||
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|- | Amino Acid Sequence; Bacterial Proteins/physiology; Chromosomes, Bacterial/ultrastructure; DNA, Bacterial/metabolism; DNA-Binding Proteins/isolation & purification; DNA-Binding Proteins/physiology; Escherichia coli/physiology; Histones/physiology; Molecular Sequence Data; Recombination, Genetic; Ribosomal Proteins/isolation & purification; Ribosomal Proteins/physiology; Saccharomyces cerevisiae/genetics | ||
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
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==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Latest revision as of 04:44, 15 September 2013
| Citation |
Bruckner, RC and Cox, MM (1989) The histone-like H protein of Escherichia coli is ribosomal protein S3. Nucleic Acids Res. 17:3145-61 |
|---|---|
| Abstract |
We report the purification of four proteins from Escherichia coli that stimulate or inhibit inter- and/or intramolecular recombination promoted by the yeast plasmid-encoded FLP protein. The proteins are identified as the ribosomal proteins S3 (27 kDa), L2 (26 kDa), S4 (24 kDa), and S5 (16 kDa), on the basis of N-terminal sequence analysis. The S3 protein is found to be identical to H protein, an E. coli histone-like protein that is related to histone H2A immunologically and by virtue of amino acid content. The H protein/S3 identity is based on co-migration on polyacrylamide gels, heat stability, amino acid analysis, and effects on FLP-promoted recombination. These results are relevant to current studies on the structure of the E. coli nucleoid. Since the H protein has previously been found associated with the E. coli nucleoid, the results indicate that either (a) some ribosomal proteins serve a dual function in E. coli, or, more likely, (b) ribosomal proteins can and are being mis-identified as nucleoid constituents. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/physiology; Chromosomes, Bacterial/ultrastructure; DNA, Bacterial/metabolism; DNA-Binding Proteins/isolation & purification; DNA-Binding Proteins/physiology; Escherichia coli/physiology; Histones/physiology; Molecular Sequence Data; Recombination, Genetic; Ribosomal Proteins/isolation & purification; Ribosomal Proteins/physiology; Saccharomyces cerevisiae/genetics |
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