Integration of the Thylakoid Membrane Protein Cytochromeb6in the Cytoplasmic Membrane ofEscherichia coli†

Biochemistry ◽  
2005 ◽  
Vol 44 (20) ◽  
pp. 7570-7576 ◽  
Author(s):  
Jaroslaw Króliczewski ◽  
Katarzyna Hombek-Urban ◽  
Andrzej Szczepaniak
Keyword(s):  
Membrane Protein ◽  
Thylakoid Membrane ◽  
Cytoplasmic Membrane ◽  
Ofescherichia Coli

scholarly journals The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana

2002 ◽  
Vol 368 (3) ◽  
pp. 777-781 ◽  
Author(s):  
Eva KLOSTERMANN ◽  
Imke DROSTE gen. HELLING ◽  
Jean-Pierre CARDE ◽  
Danja SCHÜNEMANN
Keyword(s):  
Arabidopsis Thaliana ◽  
Membrane Protein ◽  
Thylakoid Membrane ◽  
Cytoplasmic Membrane ◽  
Gel Filtration ◽  
Direct Interaction ◽  
Electron Microscopic ◽  
Thylakoid Membrane Proteins ◽  
Oligomeric Complex ◽  
Blue Native

The integration of light-harvesting chlorophyll proteins (LHCPs) into the thylakoid membrane requires the integral thylakoid membrane protein ALB3, a homologue of the bacterial cytoplasmic membrane protein YidC. In bacteria, YidC is associated with the SecY-translocase and facilitates the integration of Sec-dependent proteins into the plasma membrane. In addition, it is also involved in the insertion of Sec-independent proteins. In the present study we demonstrate, in Arabidopsis thaliana, that most ALB3 is a constituent of an oligomeric complex of approx. 180kDa. In addition, we detected ALB3 in several higher-molecular-mass complexes (up to 700kDa). Furthermore, we show that most ALB3 co-fractionates with cpSecY during gel-filtration analysis and blue native gel electrophoresis, suggesting an association of ALB3 with the cpSecY complex. A direct interaction of ALB3 with the cpSecY complex was demonstrated by co-immunoprecipitation experiments using digitonin-solubilized thylakoid membrane proteins and anti-cpSecY or anti-ALB3 antibodies. This result was further confirmed by electron microscopic co-immunolocalization of ALB3 and cpSecY. In addition, an association of ALB3 with the cpSecY complex was demonstrated directly by cross-linking experiments using the chemical cross-linker disuccinimidyl suberate.

scholarly journals The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli.

1992 ◽  
Vol 267 (8) ◽  
pp. 5339-5345
Author(s):  
B Traxler ◽  
C Lee ◽  
D Boyd ◽  
J Beckwith
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Cytoplasmic Membrane

scholarly journals Cloning and Characterization of theFlavobacterium johnsoniae Gliding Motility GenesgldD and gldE

2001 ◽  
Vol 183 (14) ◽  
pp. 4167-4175 ◽  
Author(s):  
David W. Hunnicutt ◽  
Mark J. McBride
Keyword(s):  
Membrane Protein ◽  
Cytoplasmic Membrane ◽  
Sequence Similarity ◽  
Gliding Motility ◽  
Wild Type ◽  
Bacteriophage Infection ◽  
Flavobacterium Johnsoniae ◽  
Latex Spheres ◽  
Serovar Typhimurium

ABSTRACT Cells of Flavobacterium johnsoniae move over surfaces by a process known as gliding motility. The mechanism of this form of motility is not known. Cells of F. johnsoniaepropel latex spheres along their surfaces, which is thought to be a manifestation of the motility machinery. Three of the genes that are required for F. johnsoniae gliding motility,gldA, gldB, and ftsX, have recently been described. Tn4351 mutagenesis was used to identify another gene, gldD, that is needed for gliding. Tn4351-induced gldD mutants formed nonspreading colonies, and cells failed to glide. They also lacked the ability to propel latex spheres and were resistant to bacteriophages that infect wild-type cells. Introduction of wild-type gldD into the mutants restored motility, ability to propel latex spheres, and sensitivity to bacteriophage infection. gldD codes for a cytoplasmic membrane protein that does not exhibit strong sequence similarity to proteins of known function. gldE, which lies immediately upstream ofgldD, encodes another cytoplasmic membrane protein that may be involved in gliding motility. Overexpression ofgldE partially suppressed the motility defects of agldB point mutant, suggesting that GldB and GldE may interact. GldE exhibits sequence similarity to Borrelia burgdorferi TlyC and Salmonella enterica serovar Typhimurium CorC.

Patching plasma membrane disruptions with cytoplasmic membrane

2000 ◽  
Vol 113 (11) ◽  
pp. 1891-1902 ◽  
Author(s):  
P.L. McNeil ◽  
S.S. Vogel ◽  
K. Miyake ◽  
M. Terasaki
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Sea Urchin ◽  
Membrane Trafficking ◽  
Cytoplasmic Membrane ◽  
Yolk Granule ◽  
High Threshold ◽  
Surface Markers ◽  
Plasma Membrane Protein ◽  
Cell Cytoplasm

Vesicle-vesicle fusion initiated in cell cytoplasm by high Ca(2+) can rapidly erect large membrane boundaries. These might be used as a ‘patch’ for resealing plasma membrane disruptions. Three central predictions of this ‘patch’ hypothesis are here established in sea urchin eggs. First, we show that surface markers for plasma membrane protein and lipid are initially absent over disruption sites after resealing is complete. Second, we demonstrate that resealing capacity is strongly dependent upon local availability of fusion competent cytoplasmic organelles, specifically the reserve or yolk granule. Lastly, we demonstrate that the reserve granule is capable of rapid (t(1/2) <1 second), Ca(2+)-regulated (high threshold) fusion capable of erecting large (>1000 μm(2)), continuous membrane boundaries. Production of patch vesicles for resealing may proceed by an ‘emergency’ fusion mechanism distinct from that utilized for the much slower, highly regulated, cytosol-requiring organelle-organelle fusion events typical of constitutive membrane trafficking pathways.

scholarly journals Contribution of the FtsQ Transmembrane Segment to Localization to the Cell Division Site

2007 ◽  
Vol 189 (20) ◽  
pp. 7273-7280 ◽  
Author(s):  
Dirk-Jan Scheffers ◽  
Carine Robichon ◽  
Gert Jan Haan ◽  
Tanneke den Blaauwen ◽  
Gregory Koningstein ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Membrane Protein ◽  
Cytoplasmic Membrane ◽  
Central Component ◽  
Transmembrane Segment ◽  
Division Site ◽  
Periplasmic Domain ◽  
Cell Division Protein

ABSTRACT The Escherichia coli cell division protein FtsQ is a central component of the divisome. FtsQ is a bitopic membrane protein with a large C-terminal periplasmic domain. In this work we investigated the role of the transmembrane segment (TMS) that anchors FtsQ in the cytoplasmic membrane. A set of TMS mutants was made and analyzed for the ability to complement an ftsQ mutant. Study of the various steps involved in FtsQ biogenesis revealed that one mutant (L29/32R;V38P) failed to functionally insert into the membrane, whereas another mutant (L29/32R) was correctly assembled and interacted with FtsB and FtsL but failed to localize efficiently to the cell division site. Our results indicate that the FtsQ TMS plays a role in FtsQ localization to the division site.

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