ASP83, GLU113 AND GLU134 ARE NOT SPECIFICALLY INVOLVED IN SCHIFF-BASE PROTONATION OR WAVELENGTH REGULATION IN BOVINE RHODOPSIN

被引：23

作者：

JANSSEN, JJM

DECALUWE, GLJ

DEGRIP, WJ

机构：

[1] Department of Biochemistry, University of Nijmegen, 6500 HB Nijmegen

来源：

FEBS LETTERS | 1990年 / 260卷 / 01期

关键词：

Amino acid substitution; Baculovirus; Heterologous expression; Rhodopsin; Site selective mutagenesis; Spectral property;

D O I：

10.1016/0014-5793(90)80080-3

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：

Site-specific mutagenesis was employed to investigate the proposed contribution of proton-donating residues (Glu, Asp) in the membrane domains of bovine rhodopsin to protonation of the Schiff base-linking protein and chromophore or to wavelength modulation of this visual pigment. Three point-mutations were introduced to replace the highly conserved residues Asp83 by Asn (D83N), Glu113 by Gln (E113Q) or Glu134 by Asp (E134D), respectively. All 3 substitutions had only marginal effects on the spectral properties of the final pigment (≤ 3 nm blue-shift relative to native rhodopsin). Hence, none of these residues by itself is specifically involved in Schiff base protonation or wavelength modulation of bovine rhodopsin. © 1990.

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页码：113 / 118

页数：6

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