LOCALIZATION OF SURFACE PEPTIDE FROM RIBOSOMAL PROTEIN-L7 ON 80S RIBOSOME BY BIOTINYLATION

被引：14
|
作者：
LIN, A
机构：
[1] Institute of Genetics, National Yang-Ming Medical College, Taipei, Shih-Pai
来源：
FEBS LETTERS | 1991年 / 287卷 / 1-2期
关键词：
BIOTINYLATION; RIBOSOMAL PROTEIN; RIBOSOMAL PEPTIDE; N'; HYDROXYSUCCINIMIDO-BIOTIN; (NHS-BIOTIN);
D O I：
10.1016/0014-5793(91)80030-7
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 surface topography of ribosomal peptides on ribosome particles was conducted by using N',Hydroxysuccinimido-biotin (NHS-biotin) modification. All rat ribosomal proteins, except proteins L3 and L8, are biotinylated when the ribosome particle is the substrate. A surface peptide from protein L7 was determined from biotinylated ribosomes by high performance liquid chromatography and cyanogen bromide peptide mapping. It was found that only the tandem repeats of the NH2-terminal segment of protein L7 are accessible to biotinylation. It is concluded that the NH2-terminal-end of protein L7 should be exposed on the surface of ribosomal particles.
引用
收藏
页码：121 / 124
页数：4
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