首页    期刊浏览 2024年09月06日 星期五
登录注册

文章基本信息

  • 标题:Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane
  • 本地全文:下载
  • 作者:S Inouye ; S Wang ; J Sekizawa
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1977
  • 卷号:74
  • 期号:3
  • 页码:1004-1008
  • DOI:10.1073/pnas.74.3.1004
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:The messenger RNA for the lipoprotein of the E. coli outer membrane was found to code for a putative precursor, prolipoprotein, which has 20 additional amino acid residues extending from the amino terminus of the lipoprotein. Using the prolipoprotein synthesized in an E. coli cell-free system directed by purified messenger RNA for the lipoprotein, the complete amino acid sequence of the amino-terminal precursor region was determined to be as follows: (formula: see text). It was also found that the prolipoprotein that accumulates in toluene-treated cells has the same sequence. The significance of the amino acid sequence is discussed in terms of the mechanism of biosynthesis and assembly of the lipoprotein in the E. coli outer membrane.
国家哲学社会科学文献中心版权所有