Conserved cytoplasmic motifs that distinguish sub-groups of the polyprenol phosphate:: N-acetylhexosamine-1-phosphate transferase family

被引:42
作者
Anderson, MS
Eveland, SS
Price, NPJ
机构
[1] Merck Res Labs, Dept Enzymol & Prot Biochem, Rahway, NJ 07065 USA
[2] SUNY Coll Environm Sci & Forestry, Dept Chem, Syracuse, NY 13210 USA
关键词
sugar nucleotide; mra Y; WecA; WbcO; tunicamycin;
D O I
10.1016/S0378-1097(00)00385-2
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
WecA, MraY and WbcO are conserved members of the polyprenol phosphate: N-acetylhexosamine-1-phosphate transferase family involved in the assembly of bacterial cell walls, and catalyze reactions involving a membrane-associated polyprenol phosphate acceptor substrate and a cytoplasmically located UDP-D-amino sugar donor. MraY, WbcO and WecA purportedly utilize different UDP-sugars, although the molecular basis of this specificity is largely unknown. However, domain variations involved in specificity are predicted to occur on the cytoplasmic side of the membrane, adjacent to conserved domains involved in the mechanistic activity, and with access to the cytoplasmically located sugar nucleotides. Conserved C-terminal domains have been identified that satisfy these criteria. Topological,analyses indicate that they form the highly basic, fifth cytoplasmic loop between transmembrane regions IX and X. Four diverse loops are apparent, for MraY, WecA, WbcO and RgpG, that uniquely characterize these sub-groups of the transferase family, and a correlation is evident with the known or implied UDP-sugar specificity. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:169 / 175
页数:7
相关论文
共 23 条
[1]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[2]   Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis [J].
Bouhss, A ;
Mengin-Lecreulx, D ;
Le Beller, D ;
van Heijenoort, J .
MOLECULAR MICROBIOLOGY, 1999, 34 (03) :576-585
[3]   Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: Inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli [J].
Brandish, PE ;
Kimura, K ;
Inukai, M ;
Southgate, R ;
Lonsdale, JT ;
Bugg, TDH .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1996, 40 (07) :1640-1644
[4]  
BUGG TDH, 1994, FEMS MICROBIOL LETT, V119, P255
[5]   THE FINAL STEP OF PEPTIDOGLYCAN SUBUNIT ASSEMBLY IN ESCHERICHIA-COLI OCCURS IN THE CYTOPLASM [J].
BUPP, K ;
VANHEIJENOORT, J .
JOURNAL OF BACTERIOLOGY, 1993, 175 (06) :1841-1843
[6]   Recent improvements of the ProDom database of protein domain families [J].
Corpet, F ;
Gouzy, J ;
Kahn, D .
NUCLEIC ACIDS RESEARCH, 1999, 27 (01) :263-267
[7]   Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method [J].
Cserzo, M ;
Wallin, E ;
Simon, I ;
vonHeijne, G ;
Elofsson, A .
PROTEIN ENGINEERING, 1997, 10 (06) :673-676
[8]   Conserved sequences in enzymes of the UDP-GlcNAc/MurNAc family are essential in hamster UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase [J].
Dal Nogare, AR ;
Dan, N ;
Lehrman, MA .
GLYCOBIOLOGY, 1998, 8 (06) :625-632
[9]   Hamster UDP-N-acetylglucosamine:dolichol-P N-acetylglucosamine-1-P transferase has multiple transmembrane spans and a critical cytosolic loop [J].
Dan, N ;
Middleton, RB ;
Lehrman, MA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (48) :30717-30724
[10]   WHOLE-GENOME RANDOM SEQUENCING AND ASSEMBLY OF HAEMOPHILUS-INFLUENZAE RD [J].
FLEISCHMANN, RD ;
ADAMS, MD ;
WHITE, O ;
CLAYTON, RA ;
KIRKNESS, EF ;
KERLAVAGE, AR ;
BULT, CJ ;
TOMB, JF ;
DOUGHERTY, BA ;
MERRICK, JM ;
MCKENNEY, K ;
SUTTON, G ;
FITZHUGH, W ;
FIELDS, C ;
GOCAYNE, JD ;
SCOTT, J ;
SHIRLEY, R ;
LIU, LI ;
GLODEK, A ;
KELLEY, JM ;
WEIDMAN, JF ;
PHILLIPS, CA ;
SPRIGGS, T ;
HEDBLOM, E ;
COTTON, MD ;
UTTERBACK, TR ;
HANNA, MC ;
NGUYEN, DT ;
SAUDEK, DM ;
BRANDON, RC ;
FINE, LD ;
FRITCHMAN, JL ;
FUHRMANN, JL ;
GEOGHAGEN, NSM ;
GNEHM, CL ;
MCDONALD, LA ;
SMALL, KV ;
FRASER, CM ;
SMITH, HO ;
VENTER, JC .
SCIENCE, 1995, 269 (5223) :496-512