RIBOSOMES IN THIOSTREPTON-RESISTANT MUTANTS OF BACILLUS-MEGATERIUM LACKING A SINGLE 50-S SUBUNIT PROTEIN

被引:77
作者
CUNDLIFFE, E
DIXON, P
STARK, M
STOFFLER, G
EHRLICH, R
STOFFLERMEILICKE, M
CANNON, M
机构
[1] MAX PLANCK INST MOLEC GENET,WITTMANN ABT,D-1000 BERLIN 33,FED REP GER
[2] UNIV LONDON KINGS COLL,DEPT BIOCHEM,LONDON WC2R 2LS,ENGLAND
关键词
D O I
10.1016/0022-2836(79)90393-0
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
A protein required for the binding of thiostrepton to ribosomes of Bacillus megaterium has been purified and further characterized by immunological techniques. This protein, which does not bind the drug off the ribosome, is serologically-homologous to Escherichia coli ribosomal protein L11 and is designated BM-L11. Ribosomes from certain thiostrepton-resistant mutants of B. megaterium appear to be totally devoid of protein BM-L11 as judged by modified immunoelectrophoresis. Such ribosomes are significantly less sensitive than those from wild-type organisms to the action of thiostrepton in vitro but retain substantial protein synthetic activity. Re-addition of protein BM-L11 to ribosomes from the mutants restores them to wild-type levels of activity and thiostrepton sensitivity. Thus ribosomal protein BM-L11 is involved not only in binding thiostrepton but also in determining the thiostrepton phenotype. © 1979.
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页码:235 / 252
页数:18
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