Results 31 to 40 of about 34,450 (211)

Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli [PDF]

open access: yesJournal of Bacteriology, 1988
The DNA sequence of the secA gene, essential for protein export in Escherichia coli, was determined and found to encode a hydrophilic protein of 901 amino acid residues with a predicted molecular weight of 101,902, consistent with its previously determined size and subcellular location.
M G, Schmidt   +3 more
openaire   +2 more sources

Cloning and Expression Analysis of Phytoplasma Protein Translocation Genes

open access: yesMolecular Plant-Microbe Interactions, 2001
Genes encoding SecA and SecY proteins, essential components of the Sec protein translocation system, were cloned from onion yellows phytoplasma, an unculturable plant pathogenic bacterium. The secA gene consists of 2,505 nucleotides encoding an 835 amino
Shigeyuki Kakizawa   +9 more
doaj   +1 more source

In Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis. [PDF]

open access: yesPLoS ONE, 2015
The majority of proteins that are secreted across the bacterial cytoplasmic membrane leave the cell via the Sec pathway, which in its minimal form consists of the dimeric ATP-driven motor protein SecA that associates with the protein-conducting membrane ...
Irfan Prabudiansyah   +2 more
doaj   +1 more source

Multiple SecA protein isoforms in Escherichia coli [PDF]

open access: yesJournal of Bacteriology, 1987
To define the anti-SecA-LacZ antiserum, immunoprecipitates produced with either whole anti-SecA-LacZ rabbit antiserum or affinity-purified antibodies were used to analyze nondenatured lysates of Escherichia coli. The antiserum contains antibodies that recognize different proteins.
openaire   +2 more sources

The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity

open access: yeseLife, 2019
In bacteria, the translocation of proteins across the cytoplasmic membrane by the Sec machinery requires the ATPase SecA. SecA binds ribosomes and recognises nascent substrate proteins, but the molecular mechanism of nascent substrate recognition is ...
Mohammed Jamshad   +10 more
doaj   +1 more source

Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex [PDF]

open access: yes, 2012
The bacterial ATPase SecA and protein channel complex SecYEG form the core of an essential protein translocation machinery. The nature of the conformational changes induced by each stage of the hydrolytic cycle of ATP and how they are coupled to protein ...
Alice Robson   +42 more
core   +2 more sources

Conformational Dynamics of the Plug Domain of the SecYEG Protein-conducting Channel [PDF]

open access: yes, 2011
The central pore of the SecYEG preprotein-conducting channel is closed at the periplasmic face of the membrane by a plug domain. To study its conformational dynamics, the plug was labeled site-specifically with an environment-sensitive fluorophore.
Arkowitz   +44 more
core   +2 more sources

SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane [PDF]

open access: yesThe EMBO Journal, 1997
SecA, the preprotein-driving ATPase in Escherichia coli, was shown previously to insert deeply into the plasma membrane in the presence of ATP and a preprotein; this movement of SecA was proposed to be mechanistically coupled with preprotein translocation.
G, Matsumoto, T, Yoshihisa, K, Ito
openaire   +2 more sources

Voltage Sensing in Bacterial Protein Translocation [PDF]

open access: yes, 2020
The bacterial channel SecYEG efficiently translocates both hydrophobic and hydrophilic proteins across the plasma membrane. Translocating polypeptide chains may dislodge the plug, a half helix that blocks the permeation of small molecules, from its ...
Bondar, Ana-Nicoleta   +5 more
core   +1 more source

Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome

open access: yesmBio, 2019
Bacteria execute a variety of protein transport systems for maintaining the proper composition of their different cellular compartments. The SecYEG translocon serves as primary transport channel and is engaged in transporting two different substrate ...
Lara Knüpffer   +5 more
doaj   +1 more source

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