Combination of Trp and Glu residues for recognition of mRNA cap structure Analysis of m7G base recognition site of human cap binding protein (IF‐4E) by site‐directed mutagenesis

FEBS Letters

Morioka, Hiroshi³  Uesugi, Seiichi²  Iyo, Hiromi¹  Doi, Mitsunobu¹  Inoue, Masatoshi¹  Ueda, Hitoshi¹  Ishida, Toshimasa¹  Nishikawa, Satoshi⁴  Tanaka, Toshiki⁵ 

[1] Osaka University of Pharmaceutical Sciences, 2-10-65 Kawai, Matsubara, Osaka 580, Japan;Faculty of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka, 565, Japan;Faculty of Pharmaceutical Sciences, Hokkaido University, Kita 12 Nishi 6 Kitaku, Sapporo 060, Japan;Fermentation Research Institute, Agency of Industrial Science and Technology, MITI, 1-1-3 Higashi, Tsukuba 305, Japan;Protein Engineering Research Institute, 6-2-1 Furuedai, Suita, Japan

关键词: Human cap binding protein;    Cassette mutagenesis;    Cap binding activity;    hCBP;    human cap binding protein;    hGH;    human growth hormone;    IAA;    3-indoleacrylic acid;   

DOI  :  10.1016/0014-5793(91)80294-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown