A protein residing at the subunit interface of the bacterial ribosome

被引:85
作者
Agafonov, DE
Kolb, VA
Nazimov, IV
Spirin, AS [1 ]
机构
[1] Russian Acad Sci, Inst Prot Res, Pushchino 142292, Moscow Region, Russia
[2] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117871, Russia
关键词
ribosomal proteins; ribosome dissociation; ribosomal surface; tritium labeling;
D O I
10.1073/pnas.96.22.12345
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Surface labeling of Escherichia coli ribosomes with the use of the tritium bombardment technique has revealed a minor unidentified ribosome-bound protein (spot Y) that is hidden in the 70S ribosome and becomes highly labeled on dissociation of the 70S ribosome into subunits. In the present work, the N-terminal sequence of the protein Y was determined and its gene was identified as yfia, an ORF located upstream the phe operon of E. coli. This 12.7-kDa protein was isolated and characterized. An affinity of the purified protein Y for the 30S subunit, but not for the 50S ribosomal subunit, was shown. The protein proved to be exposed on the surface of the 30S subunit. The attachment of the 50S subunit resulted in hiding the protein Y, thus suggesting the protein location at the subunit interface in the 70S ribosome. The protein was shown to stabilize ribosomes against dissociation. The possible role of the protein Y as ribosome association factor in translation is discussed.
引用
收藏
页码:12345 / 12349
页数:5
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