Bruckner R C, Cox M M
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, Madison 53706.
Nucleic Acids Res. 1989 Apr 25;17(8):3145-61. doi: 10.1093/nar/17.8.3145.
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.
我们报道了从大肠杆菌中纯化出的四种蛋白质，它们可刺激或抑制酵母质粒编码的FLP蛋白促进的分子间和/或分子内重组。根据N端序列分析，这些蛋白质被鉴定为核糖体蛋白S3（27 kDa）、L2（26 kDa）、S4（24 kDa）和S5（16 kDa）。发现S3蛋白与H蛋白相同，H蛋白是一种大肠杆菌类组蛋白，在免疫学上以及根据氨基酸含量与组蛋白H2A相关。H蛋白与S3的同一性基于在聚丙烯酰胺凝胶上的共迁移、热稳定性、氨基酸分析以及对FLP促进的重组的影响。这些结果与目前关于大肠杆菌类核结构的研究相关。由于此前已发现H蛋白与大肠杆菌类核相关，结果表明要么（a）某些核糖体蛋白在大肠杆菌中具有双重功能，或者更有可能的是，（b）核糖体蛋白可能且正在被错误地鉴定为类核成分。
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