A family of Gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from Gram-negative bacteria

被引:217
作者
Paulsen, IT [1 ]
Park, JH [1 ]
Choi, PS [1 ]
Saier, MH [1 ]
机构
[1] Univ Calif San Diego, Dept Biol, La Jolla, CA 92093 USA
关键词
transport; outer membrane; beta-barrel; Gram-negative bacteria; active export; protein; complex carbohydrate; drug; heavy metal;
D O I
10.1111/j.1574-6968.1997.tb12697.x
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Gram-negative bacteria have evolved transport complexes that export macromolecules and toxic substances across the two membranes of the cell envelope in a single energy coupled step. The process requires (1) a cytoplasmic membrane export system, (2) a membrane fusion protein (MFP), and (3) an outer membrane factor (OMF). Families comprising the former two constituents have been described previously. We here present an analysis of the phylogenetic and structural characteristics of the OMF family. Twenty-one members of this family have been identified, and based on available evidence, they function in conjunction with ABC, RND, MFS and/or other types of cytoplasmic transport systems. OMFs exhibit fairly uniform sizes (398-495 residues with two exceptions), and based on computational analyses, they may form beta-barrel structures consisting of up to 16 beta-strands. Phylogenetic analyses reveal that while the MFPs cluster in accordance with the type of cytoplasmic membrane transport systems with which they function, OMFs do not. We conclude that OMFs probably comprise a family of outer membrane porin-type proteins of uniform structure which did not coevolve with their cognate cytoplasmic membrane transport systems.
引用
收藏
页码:1 / 8
页数:8
相关论文
共 28 条
[1]  
ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1006/jmbi.1990.9999
[2]   PROSITE - A DICTIONARY OF SITES AND PATTERNS IN PROTEINS [J].
BAIROCH, A .
NUCLEIC ACIDS RESEARCH, 1992, 20 :2013-2018
[3]   EMPIRICAL PREDICTIONS OF PROTEIN CONFORMATION [J].
CHOU, PY ;
FASMAN, GD .
ANNUAL REVIEW OF BIOCHEMISTRY, 1978, 47 :251-276
[4]   CRYSTAL-STRUCTURES EXPLAIN FUNCTIONAL-PROPERTIES OF 2 ESCHERICHIA-COLI PORINS [J].
COWAN, SW ;
SCHIRMER, T ;
RUMMEL, G ;
STEIERT, M ;
GHOSH, R ;
PAUPTIT, RA ;
JANSONIUS, JN ;
ROSENBUSCH, JP .
NATURE, 1992, 358 (6389) :727-733
[5]   A COMPREHENSIVE SET OF SEQUENCE-ANALYSIS PROGRAMS FOR THE VAX [J].
DEVEREUX, J ;
HAEBERLI, P ;
SMITHIES, O .
NUCLEIC ACIDS RESEARCH, 1984, 12 (01) :387-395
[6]   A FAMILY OF EXTRACYTOPLASMIC PROTEINS THAT ALLOW TRANSPORT OF LARGE MOLECULES ACROSS THE OUTER MEMBRANES OF GRAM-NEGATIVE BACTERIA [J].
DINH, T ;
PAULSEN, IT ;
SAIER, MH .
JOURNAL OF BACTERIOLOGY, 1994, 176 (13) :3825-3831
[7]   CZC/CNR EFFLUX - A 3-COMPONENT CHEMIOSMOTIC ANTIPORT PATHWAY WITH A 12-TRANSMEMBRANE-HELIX PROTEIN [J].
DONG, QH ;
MERGEAY, M .
MOLECULAR MICROBIOLOGY, 1994, 14 (01) :185-187
[8]  
Doolittle R.F., 1986, Of Urfs and Orfs: A Primer on How to Analyze Derived Amino Acid Sequences
[9]   ABC TRANSPORTERS - BACTERIAL EXPORTERS [J].
FATH, MJ ;
KOLTER, R .
MICROBIOLOGICAL REVIEWS, 1993, 57 (04) :995-1017
[10]  
FENG DF, 1990, METHOD ENZYMOL, V183, P375