FMN is covalently attached to a threonine residue in the NqrB and NqrC subunits of Na+-translocating NADH-quinone reductase from Vibrio alginolyticus

被引:76
作者
Hayashi, M
Nakayama, Y
Yasui, M
Maeda, M
Furuishi, K
Unemoto, T
机构
[1] Chiba Univ, Fac Pharmaceut Sci, Lab Membrane Biochem, Inage Ku, Chiba 2638522, Japan
[2] Appl Biosyst Japan, Chuo Ku, Tokyo 1040032, Japan
关键词
covalently bound flavin; FMN; Na+-translocating NADH-quinone reductase; threonine; matrix-assisted laser desorption ionization time-of-flight mass spectrometry; Vibrio alginolyticus;
D O I
10.1016/S0014-5793(00)02404-2
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
The Na+-translocating NADH-quinone reductase (NQR) from Vibrio alginolyticus is composed of six subunits (NqrA to NqrF). We previously demonstrated that both NqrB and NqrC subunits contain a flavin cofactor covalently attached to a threonine residue. Fluorescent peptide fragments derived from the NqrB and NqrC subunits mere applied to a matrix-assisted laser desorption ionization time-of-flight mass spectrometer, and covalently attached flavin was identified as FMN in both subunits, From post-source decay fragmentation analysis, it was concluded that FMN is attached by a phosphate group to Thr-235 in the NqrB subunit and to Thr-223 in the NqrC subunit, The phosphoester binding of FMN to a threonine residue reported here is a new type of flavin attachment to a polypeptide. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:5 / 8
页数:4
相关论文
共 11 条
[1]   CLONING AND SEQUENCING OF 4 STRUCTURAL GENES FOR THE NA+-TRANSLOCATING NADH-UBIQUINONE OXIDOREDUCTASE OF VIBRIO-ALGINOLYTICUS [J].
BEATTIE, P ;
TAN, K ;
BOURNE, RM ;
LEACH, D ;
RICH, PR ;
WARD, FB .
FEBS LETTERS, 1994, 356 (2-3) :333-338
[2]   CLONING OF THE NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE GENE FROM THE MARINE BACTERIUM VIBRIO-ALGINOLYTICUS AND THE EXPRESSION OF THE BETA-SUBUNIT IN ESCHERICHIA-COLI [J].
HAYASHI, M ;
HIRAI, K ;
UNEMOTO, T .
FEBS LETTERS, 1994, 356 (2-3) :330-332
[3]   SEQUENCING AND THE ALIGNMENT OF STRUCTURAL GENES IN THE NQR OPERON ENCODING THE NA+-TRANSLOCATING NADH-QUINONE REDUCTASE FROM VIBRIO-ALGINOLYTICUS [J].
HAYASHI, M ;
HIRAI, K ;
UNEMOTO, T .
FEBS LETTERS, 1995, 363 (1-2) :75-77
[4]   SUBUNIT COMPONENT AND THEIR ROLES IN THE SODIUM-TRANSPORT NADH-QUINONEREDUCTASE OF A MARINE BACTERIUM, VIBRIO-ALGINOLYTICUS [J].
HAYASHI, M ;
UNEMOTO, T .
BIOCHIMICA ET BIOPHYSICA ACTA, 1987, 890 (01) :47-54
[5]   FAD AND FMN FLAVOPROTEINS PARTICIPATE IN THE SODIUM-TRANSPORT RESPIRATORY-CHAIN NADH QUINONE REDUCTASE OF A MARINE BACTERIUM, VIBRIO-ALGINOLYTICUS [J].
HAYASHI, M ;
UNEMOTO, T .
FEBS LETTERS, 1986, 202 (02) :327-330
[6]   Covalently bound flavin in the NqrB and NqrC subunits of Na+-translocating NADH-quinone reductase from Vibrio alginolyticus [J].
Nakayama, Y ;
Yasui, M ;
Sugahara, K ;
Hayashi, M ;
Unemoto, T .
FEBS LETTERS, 2000, 474 (2-3) :165-168
[7]   Identification of six subunits constituting Na+-translocating NADH-quinone reductase from the marine Vibrio alginolyticus [J].
Nakayama, Y ;
Hayashi, M ;
Unemoto, T .
FEBS LETTERS, 1998, 422 (02) :240-242
[8]   THE NA+-TRANSLOCATING NADH-UBIQUINONE OXIDOREDUCTASE FROM THE MARINE BACTERIUM VIBRIO-ALGINOLYTICUS CONTAINS FAD BUT NOT FMN [J].
PFENNINGERLI, XD ;
DIMROTH, P .
FEBS LETTERS, 1995, 369 (2-3) :173-176
[9]   NA+-TRANSLOCATING NADH-QUINONE REDUCTASE OF MARINE AND HALOPHILIC BACTERIA [J].
UNEMOTO, T ;
HAYASHI, M .
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 1993, 25 (04) :385-391
[10]  
UNEMOTO T, 1990, BACTERIA, V12, P33