Characterization of pores formed by YaeT (Omp85) from Escherichia coli

被引:47
作者
Stegmeier, Johannes F. [1 ]
Andersen, Christian [1 ]
机构
[1] Univ Wurzburg, Biozentrum, Lehrstuhl Biotechnol, D-97074 Wurzburg, Germany
关键词
bacterial outer membrane; membrane biogenesis; Omp85; reconstitution in black lipid membranes;
D O I
10.1093/jb/mvj147
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
Proteins of the Omp85 family play a major role in the biogenesis of the bacterial outer membrane, since they were shown to mediate insertion of outer membrane proteins. The Escherichia coli Omp85 homologue YaeT is essential for viability, but its exact mode of action is not yet elucidated. We could show that YaeT is composed of two distinct domains, an amino-terminal periplasmic and a carboxy-terminal membrane domain. The full length YaeT and the isolated membrane domain induce pores when reconstituted in planar lipid membranes. The pores exhibit a certain variability of conductance indicating a flexible structure, which could be an essential property of a lateral opening channel releasing proteins into the bacterial outer membrane. We could further show that the periplasmic domain proves to be essential for in vivo function of YaeT.
引用
收藏
页码:275 / 283
页数:9
相关论文
共 55 条
[1]   pH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding [J].
Andersen, C ;
Schiffler, B ;
Charbit, A ;
Benz, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (44) :41318-41325
[2]   Electrophysiological behavior of the TolC channel-tunnel in planar lipid bilayers [J].
Andersen, C ;
Hughes, C ;
Koronakis, V .
JOURNAL OF MEMBRANE BIOLOGY, 2002, 185 (01) :83-92
[3]   In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K-12 maltoporin:: contribution to maltose and maltooligosaccharide transport and binding [J].
Andersen, C ;
Bachmeyer, C ;
Täuber, H ;
Benz, R ;
Wang, JA ;
Michel, V ;
Newton, SMC ;
Hofnung, M ;
Charbit, A .
MOLECULAR MICROBIOLOGY, 1999, 32 (04) :851-867
[4]   A rapid selective extraction procedure for the outer membrane protein (OmpF) from Escherichia coli [J].
Arcidiacono, S ;
Butler, MA ;
Mello, CM .
PROTEIN EXPRESSION AND PURIFICATION, 2002, 25 (01) :134-137
[5]   MAJOR HEAT-MODIFIABLE OUTER-MEMBRANE PROTEIN IN GRAM-NEGATIVE BACTERIA - COMPARISON WITH THE OMPA PROTEIN OF ESCHERICHIA-COLI [J].
BEHER, MG ;
SCHNAITMAN, CA ;
PUGSLEY, AP .
JOURNAL OF BACTERIOLOGY, 1980, 143 (02) :906-913
[6]   IONIC SELECTIVITY OF PORES FORMED BY THE MATRIX PROTEIN (PORIN) OF ESCHERICHIA-COLI [J].
BENZ, R ;
JANKO, K ;
LAUGER, P .
BIOCHIMICA ET BIOPHYSICA ACTA, 1979, 551 (02) :238-247
[7]   FORMATION OF LARGE, ION-PERMEABLE MEMBRANE CHANNELS BY MATRIX PROTEIN (PORIN) OF ESCHERICHIA-COLI [J].
BENZ, R ;
JANKO, K ;
BOOS, W ;
LAUGER, P .
BIOCHIMICA ET BIOPHYSICA ACTA, 1978, 511 (03) :305-319
[8]   PERMEATION OF HYDROPHILIC MOLECULES THROUGH THE OUTER-MEMBRANE OF GRAM-NEGATIVE BACTERIA - REVIEW ON BACTERIAL PORINS [J].
BENZ, R ;
BAUER, K .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1988, 176 (01) :1-19
[9]   Structures of gram-negative cell walls and their derived membrane vesicles [J].
Beveridge, TJ .
JOURNAL OF BACTERIOLOGY, 1999, 181 (16) :4725-4733
[10]   Biogenesis of the gram-negative bacterial outer membrane [J].
Bos, MP ;
Tommassen, J .
CURRENT OPINION IN MICROBIOLOGY, 2004, 7 (06) :610-616