DESTABILIZATION OF SECONDARY STRUCTURE OF RNA BY RIBOSOMAL-PROTEIN S1 FROM ESCHERICHIA-COLI

被引：60
作者：
SZER, W
HERMOSO, JM
BOUBLIK, M
机构：
[1] NYU, SCH MED, DEPT BIOCHEM, NEW YORK, NY 10016 USA
[2] ROCHE INST MOLEC BIOL, NUTLEY, NJ 07110 USA
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1976年 / 70卷 / 03期
关键词：
D O I：
10.1016/0006-291X(76)90685-9
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：
S1 is an acidic protein associated with the 3'' end of 16S RNA; it is indispensable for ribosomal binding of natural mRNA. S1 unfolds single stranded stacked or helical polynucleotides (poly rA, poly rC, poly rU). It prevents the formation of poly (rA + rU) and poly (rI + rC) duplexes at 10-25 mM NaCl but not at 50-100 mM NaCl. Partial, salt reversible denaturation is also seen with coliphage MS2 RNA, E. coli rRNA and tRNA. Generally, only duplex structures with a Tm [melting point] > .apprx. 55.degree. C are formed in the presence of Sl. The protein unfolds single stranded DNA but not poly d(A .cntdot. T).
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页码：957 / 964
页数：8
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