COMPLEX OF ACIDIC RIBOSOMAL-PROTEINS - EVIDENCE OF A 4-TO-ONE COMPLEX OF PROTEINS IN BACILLUS-STEAROTHERMOPHILUS RIBOSOME

被引：16

作者：

MARQUIS, D ^{[1
]}

FAHNESTOCK, SR ^{[1
]}

机构：

[1] PENN STATE UNIV,DEPT BIOCHEM & BIOPHYS,UNIVERSITY PK,PA 16802

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1978年 / 119卷 / 04期

关键词：

D O I：

10.1016/0022-2836(78)90202-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two acidic proteins from the 50 S subunit of Bacillus stearothermophilus ribosomes, namely B-L13 (homologous to Escherichia coli protein L7 L12) and B-L8, form a complex. Radioactive B-L13, added to ribosomes before dissociation, does not appear in the complex after electrophoresis, so the (B-L13 · B-L8) complex must exist in the ribosome before dissociation. Digestion of B. stearothermophilus ribosomes with polyacrylamide-bound trypsin causes the appearance of new B-L8 and B-L13 spots on two-dimensional polyacrylamide gel electrophoresis, in a pattern which suggests that single molecules of B-L13 are being sequentially cleaved from a four-to-one complex of B-L13 and B-L8. © 1978.

引用

页码：557 / 567

页数：11

共 32 条

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