COMBINATION OF TRP AND GLU RESIDUES FOR RECOGNITION OF MESSENGER-RNA CAP STRUCTURE - ANALYSIS OF M7G BASE RECOGNITION SITE OF HUMAN CAP BINDING-PROTEIN (IF-4E) BY SITE-DIRECTED MUTAGENESIS

被引:27
作者
UEDA, H
IYO, H
DOI, M
INOUE, M
ISHIDA, T
MORIOKA, H
TANAKA, T
NISHIKAWA, S
UESUGI, S
机构
[1] OSAKA UNIV PHARMACEUT SCI,2-10-65 KAWAI,OSAKA 580,JAPAN
[2] MINIST INT TRADE & IND,AGCY IND SCI & TECHNOL,FERMENTAT RES INST,TSUKUBA 305,JAPAN
[3] OSAKA UNIV,FAC PHARMACEUT SCI,SUITA,OSAKA 565,JAPAN
[4] HOKKAIDO UNIV,FAC PHARMACEUT SCI,KITA KU,SAPPORO,HOKKAIDO 060,JAPAN
[5] PROT ENGN RES INST,SUITA,JAPAN
关键词
HUMAN CAP BINDING PROTEIN; CASSETTE MUTAGENESIS; CAP BINDING ACTIVITY;
D O I
10.1016/0014-5793(91)80294-D
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
Four mutants of the human cap binding protein (hCBP), in which Trp-102, Glu-103, Asp-104 or Glu-105 was changed to the aliphatic Leu or Ala, were prepared, and their cap binding abilities were examined. Cap binding abilities of two mutants, W102L (Trp-102 --> Leu) and E105A (Glu-105 --> Ala), were significantly decreased in comparison with the wild-type hCBP. This result suggest that Trp-102 and Glu-105 are both necessary for the cap binding, and the most probable binding mode with the m7G of cap structure is the combination of the stacking by Trp-102 and the hydrogen-bond pairing by Glu-105, as was already proposed from the model studies.
引用
收藏
页码:207 / 210
页数:4
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