Calcium-dependent solvation of the myristoyl group of recoverin.
Calcium-dependent solvation of the myristoyl group of recoverin.
复制标题
恢复素肉豆蔻酰基的钙依赖性溶剂化。
DOI:
10.1021/bi00036a013
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发表时间:
1995
期刊:
影响因子:
2.9
通讯作者:
Hurley,JB
中科院分区:
文献类型:
--
作者:
Hughes,RE;Brzovic,PS;Klevit,RE;Hurley,JB
Revised Manuscript Received June 26, 1995® abstract; Recoverin is an/V-myristoylated calcium-binding protein present in the photoreceptor cells of the mammalian retina. It is believed to function as a calcium sensor in visual signal transduction by coupling the kinetics of the recovery phase of the photoresponse to changes in the levels of intracellular Ca2+. Upon binding Ca2+, recoverin undergoes a conformational change that allows it to associate with membranes in a manner that requires iV-myristoyl modification. It has beenproposed that, in the Ca2+-free conformation, the myristoyl group is sequestered in a hydrophobic part of the protein, and in the Ca2+-bound conformation, the myristoyl group is exposed to solution. The crystal structure of Ca2+-bound recoverin reveals an exposed cluster of hydrophobic residues, raising the possibility that residues in this region may function as part of an intramolecular myristoyl binding site. Fluorescence spectroscopy analysis of interactions between recoverin and l-anilinonaphthalene-8-sulfonate (ANS) shows that an increase in solvent-accessible hydrophobic surface accompanies Ca2+ binding.’H nuclear magnetic resonance(NMR) spectra of myristoyl protonsshow dispersed chemical shifts in the Ca2+-free conformation that become relatively uniform upon the addition of Ca2+. Two-dimensional nuclear Overhauser effect (NOE) spectra of Ca2+-free recoverin show NOE contacts between myristoyl protons and aromatic ring protons. Tryptophan fluorescence quenching by acrylamide indicates that the myristoyl group is in proximity to a tryptophan residue only in the Ca2+-free conformation. These results indicate that the myristoyl group is in contact with residues in the hydrophobic cluster in Ca2+-free recoverin and that it is exposed to solution in the Ca2+-bound conformation.Recoverin, an N-myristoylated protein present in the rod cells of the mammalian retina, has been demonstrated to play a role in regulating cellular responses to changes in levels of intracellular Ca2+(Gray-Keller et al., 1993; Kawamura, 1993; Kawamura et al., 1993). Recoverin is a member of the EF-hand-containingsuperfamily of Ca2+-binding proteins whose members include calmodulin, troponin C, and calbindin Dqr. Proteins in this superfamily bind Ca2+ via the EF-hand motif, a helix-loop—helix structure which ligates a Ca2+ ion with a series of conserved oxygen-containing amino acidside chains (Strynadka & James, 1989). Recoverin itself defines a distinct subfamily of Ca2+-binding
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影响因子:
64.8
作者:
KAWAMURA, S
通讯作者:
KAWAMURA, S
DOI:
--
发表时间:
1993
期刊:
Journal of Biochemistry (Tokyo)
影响因子:
--
作者:
M. Kataoka;K. Mihara;F. Tokunaga
通讯作者:
F. Tokunaga
影响因子:
4.8
作者:
Masaaki Kobayashi;K. Takamatsu;S. Saitoh;T. Noguchi
通讯作者:
T. Noguchi
DOI:
10.1073/pnas.89.13.5705
发表时间:
1992
影响因子:
11.1
作者:
Ray,S;Zozulya,S;Niemi,GA;Flaherty,KM;Brolley,D;Dizhoor,AM;McKay,DB;Hurley,J;Stryer,L
通讯作者:
Stryer,L
DOI:
--
发表时间:
1992
期刊:
Biochemical and Biophysical Research Communications - BBRC
影响因子:
--
作者:
A. Nakano;M. Terasawa;M. Watanabe;N. Usuda;T. Morita;H. Hidaka
通讯作者:
H. Hidaka