Results 21 to 30 of about 34,551 (199)

Covalently Dimerized SecA Is Functional in Protein Translocation [PDF]

Journal of Biological Chemistry, 2005
The ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli. SecA exists as a dimer in solution, but the exact oligomeric state of SecA during membrane binding and preprotein translocation is a topic of debate.
de Keyzer, J, van der Sluis, EO, Spelbrink, REJ, Nijstad, N, de Kruijff, B, Nouwen, N, van der Does, C, Driessen, AJM, Sluis, Eli O. van der, Spelbrink, Robin E.J.   +9 more
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Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels [PDF]

Biochemical and Biophysical Research Communications, 2013
Previous studies showed that Escherichia coli membranes depleted of SecYEG are capable of translocating certain precursor proteins, but not other precursors such as pPhoA, indicating a differential requirement for SecYEG. In this study, we examined the role of SecYEG in pPhoA translocation using a purified reconstituted SecA-liposomes system.
Hao, Zhang, Ying-Hsin, Hsieh, Bor-Ruei, Lin, Liyan, Yu, Hsiuchin, Yang, Chun, Jiang, Sen-Fang, Sui, Phang C, Tai   +7 more
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SecA-dependent quality control of intracellular protein localization [PDF]

Proceedings of the National Academy of Sciences, 2003
Complex secretion machineries mediate protein translocation across cellular membranes. These machines typically recognize their substrates via signal sequences, which are required for proper targeting to the translocon. We report that during posttranslational secretion the widely conserved targeting factor SecA performs a quality-control function that ...
Eser, Markus, Ehrmann, Michael
openaire   +3 more sources

SecA localization and SecA-dependent secretion occurs at new division septa in group B Streptococcus. [PDF]

PLoS ONE, 2013
Exported proteins of Streptococcus agalactiae (GBS), which include proteins localized to the bacterial surface or secreted into the extracellular environment, are key players for commensal and pathogenic interactions in the mammalian host. These proteins
Sara Brega, Elise Caliot, Patrick Trieu-Cuot, Shaynoor Dramsi   +3 more
doaj   +1 more source

Protein Translocation: SecA–SecY Conformational Crosstalk Opens Channel [PDF]

Current Biology, 2016
A new study of the bacterial Sec translocase complex reports that ADP/ATP binding to SecA triggers multiple conformational changes in the SecYEG channel that may allow the passive directional movement of the polypeptide chain.
Andreas, Kuhn, Ross E, Dalbey
openaire   +2 more sources

Pharmacoinformatics-Based Approach for Uncovering the Quorum-Quenching Activity of Phytocompounds against the Oral Pathogen, Streptococcus mutans

Molecules, 2023
Streptococcus mutans, a gram-positive oral pathogen, is the primary causative agent of dental caries. Biofilm formation, a critical characteristic of S. mutans, is regulated by quorum sensing (QS).
Shakti Chandra Vadhana Marimuthu, Jayaprabhakaran Murugesan, Ewa Babkiewicz, Piotr Maszczyk, Murugesan Sankaranarayanan, Esakkimuthu Thangamariappan, Joseph Christina Rosy, Sureshbabu Ram Kumar Pandian, Selvaraj Kunjiappan, Vanavil Balakrishnan, Krishnan Sundar   +10 more
doaj   +1 more source

The SecA motor generates mechanical force during protein translocation [PDF]

Nature Communications, 2020
Abstract The Sec translocon moves proteins across lipid bilayers in all cells. The Sec channel enables passage of unfolded proteins through the bacterial plasma membrane, driven by the cytosolic ATPase SecA. Whether SecA generates mechanical force to overcome barriers to translocation posed by structured substrate proteins is unknown.
Riti Gupta, Dmitri Toptygin, Christian M. Kaiser   +2 more
openaire   +3 more sources

Proteins Related to the Type I Secretion System Are Associated with Secondary SecA_DEAD Domain Proteins in Some Species of Planctomycetes, Verrucomicrobia, Proteobacteria, Nitrospirae and Chlorobi. [PDF]

PLoS ONE, 2015
A number of bacteria belonging to the PVC (Planctomycetes-Verrucomicrobia-Chlamydiae) super-phylum contain unusual ribosome-bearing intracellular membranes. The evolutionary origins and functions of these membranes are unknown.
Olga K Kamneva, Saroj Poudel, Naomi L Ward   +2 more
doaj   +1 more source

SecA-Mediated Protein Translocation through the SecYEG Channel [PDF]

Microbiology Spectrum, 2019
ABSTRACT In bacteria, the Sec translocase mediates the translocation of proteins into and across the cytoplasmic membrane. It consists of a protein conducting channel SecYEG, the ATP-dependent motor SecA, and the accessory SecDF complex. Here we discuss the function and structure of the Sec translocase.
Komarudin, Amalina Ghaisani, Driessen, Arnold J M   +1 more
openaire   +3 more sources

SecA is required for membrane targeting of the cell division protein DivIVA in vivo

Frontiers in Microbiology, 2014
The conserved protein DivIVA is involved in different morphogenetic processes in Gram-positive bacteria. In Bacillus subtilis, the protein localises to the cell division site and cell poles, and functions as a scaffold for proteins that regulate division
Sven eHalbedel, Sven eHalbedel, Maki eKawai, Reinhard eBreitling, Leendert W. Hamoen, Leendert W. Hamoen   +5 more
doaj   +1 more source