scholarly journals Pentapeptide‐repeat, cytoplasmic‐membrane protein HglK influences the septal junctions in the heterocystous cyanobacterium Anabaena

2020 ◽  
Vol 113 (4) ◽  
pp. 794-806
Author(s):  
Sergio Arévalo ◽  
Enrique Flores
Keyword(s):  
Membrane Protein ◽  
Cytoplasmic Membrane ◽  
Heterocystous Cyanobacterium ◽  
Cyanobacterium Anabaena

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.

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

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.

FtsL, an Essential Cytoplasmic Membrane Protein Involved in Cell Division in Escherichia coli

1992 ◽  
Vol 174 (23) ◽  
pp. 7717-7728 ◽  
Author(s):  
Luz-Maria Guzman ◽  
James J. Barondess ◽  
Jon Beckwith
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Membrane Protein ◽  
Cytoplasmic Membrane ◽  
Topological Analysis ◽  
Growth Conditions ◽  
Bacterial Cell Division ◽  
Leucine Zippers ◽  
Protein Dimerization ◽  
Membrane Spanning

We have identified a gene involved in bacterial cell division, located immediately upstream of the ftsI gene in the min 2 region of the Escherichia coli chromosome. This gene, which we named ftsL , was detected through characterization of Tn phoA insertions in a plasmid containing this chromosomal region. Tn phoA topological analysis and fractionation of alkaline phosphatase fusion proteins indicated that the ftsL gene product is a 13.6-kDa cytoplasmic membrane protein with a cytoplasmic amino terminus, a single membrane-spanning segment, and a periplasmic carboxy terminus. The ftsL gene is essential for cell growth and division. A null mutation in ftsL resulted in inhibition of cell division, formation of long, nonseptate filaments, ultimate cessation of growth, and lysis. Under certain growth conditions, depletion of FtsL or expression of the largest ftsL-phoA fusion produced a variety of cell morphologies, including Y-shaped bacteria, indicating a possible general weakening of the cell wall. The FtsL protein is estimated to be present at about 20 to 40 copies per cell. The periplasmic domain of the protein displays a sequence with features characteristic of leucine zippers, which are involved in protein dimerization.

Glycolipozyme membrane protein integrase (MPIase): recent data

2014 ◽  
Vol 5 (5) ◽  
pp. 429-438 ◽  
Author(s):  
Ken-ichi Nishiyama ◽  
Keiko Shimamoto
Keyword(s):  
Escherichia Coli ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Structure Determination ◽  
Molecular Chaperone ◽  
Molecular Mechanisms ◽  
Cytoplasmic Membrane ◽  
Amino Sugars ◽  
Glycan Chain ◽  
Preprotein Translocation

AbstractA novel factor for membrane protein integration, from the cytoplasmic membrane of Escherichia coli, named MPIase (membrane protein integrase), has recently been identified and characterized. MPIase was revealed to be essential for the membrane integration of a subset of membrane proteins, despite that such integration reactions have been, thus far, thought to occur spontaneously. The structure determination study revealed that MPIase is a novel glycolipid comprising a glycan chain with three N-acetylated amino sugars connected to diacylglycerol through a pyrophosphate linker. As MPIase catalyzes membrane protein integration, we propose that MPIase is a glycolipozyme on the basis of its enzyme-like function. The glycan chain exhibits a molecular chaperone-like function by directly interacting with substrate membrane proteins. Moreover, MPIase also affects the dimer structure of SecYEG, a translocon, thereby significantly stimulating preprotein translocation. The molecular mechanisms of MPIase functions will be outlined.

Sign in / Sign up

Export Citation Format

Share Document