Results 191 to 200 of about 4,057 (206)
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Journal of Agricultural and Food Chemistry
Lactococcus lactis is a crucial food-grade cell factory for secreting valuable peptides and proteins primarily via the Sec-dependent pathway. YidC, a membrane insertase, facilitates protein insertion into the lipid membrane for the translocation. However,
Tiange Ma +5 more
semanticscholar +1 more source
Lactococcus lactis is a crucial food-grade cell factory for secreting valuable peptides and proteins primarily via the Sec-dependent pathway. YidC, a membrane insertase, facilitates protein insertion into the lipid membrane for the translocation. However,
Tiange Ma +5 more
semanticscholar +1 more source
Protein translocation through α-helical channels and insertases
StructureProtein translocation systems are essential for distributing proteins across various lipid membranes in cells. Cellular membranes, such as the endoplasmic reticulum (ER) membrane and mitochondrial inner membrane, require highly regulated protein translocation machineries that specifically allow the passage of protein polypeptides while blocking smaller
Jingxia Chen +3 more
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From the Sec complex to the membrane insertase YidC
bchm, 2009Abstract The key enzymes that catalyze the insertion of proteins into membranes are the Sec translocase and the YidC membrane insertase. Recent insights into the structure and functional intermediates of these enzymes have provided a first molecular glimpse of how they help the newly synthesized proteins to enter the membrane bilayer. In
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Substrate-Induced Conformational Change of the Escherichia coli Membrane Insertase YidC
Biochemistry, 2009The membrane insertase YidC from Escherichia coli reversibly binds its substrate Pf3 coat protein. The effect of this initial binding process was examined in vitro by fluorescence quenching of the tryptophan (Trp) residues of YidC which are highly sensitive fluorescent probes for changes of the protein's tertiary structure.
Sophie, Winterfeld +5 more
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Journal of the American Chemical Society, 2018
β-barrel outer membrane proteins (Omps) are key functional components of the outer membranes of Gram-negative bacteria, mitochondria, and plastids. In bacteria, their biogenesis requires the β-barrel-assembly machinery (Bam) with the central insertase ...
Jean-Baptiste Hartmann +4 more
semanticscholar +1 more source
β-barrel outer membrane proteins (Omps) are key functional components of the outer membranes of Gram-negative bacteria, mitochondria, and plastids. In bacteria, their biogenesis requires the β-barrel-assembly machinery (Bam) with the central insertase ...
Jean-Baptiste Hartmann +4 more
semanticscholar +1 more source
26 DNA Base-Insertion Enzymes (Insertases)
1981Publisher Summary DNA base-insertion enzymes (insertases) are a class of enzymes that catalyze the reinsertion of a missing base into the appropriate apurinic or apyrimidinic sites (AP sites) in DNA. The base-deoxyribose bonds in DNA are susceptible to spontaneous cleavages that release free bases and lead to the formation of apurinic or apyrimidinic
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Substrate-Dependent Conformational Dynamics of the Escherichia coli Membrane Insertase YidC
Biochemistry, 2011The binding of Pf3 coat protein to the membrane insertase YidC from Escherichia coli induces a conformational change in the tertiary structure of the insertase, resulting in a quenching of the intrinsic tryptophan (Trp) fluorescence. Tryptophan mutants of YidC were generated to examine such conformational movements in detail with time-resolved and ...
Nora, Imhof, Andreas, Kuhn, Uwe, Gerken
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Biochemical and Biophysical Research Communications - BBRC, 2021
Yindi Chu +4 more
semanticscholar +1 more source
Yindi Chu +4 more
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Structural basis of an EMC:Spf1 insertase-dislocase complex in the eukaryotic endoplasmic reticulum
bioRxivCarolin J Klose +11 more
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Consecutive steps of membrane insertion of the two-spanning MscL protein by insertase YidC.
Journal of Molecular BiologyPhilip Kauffman +3 more
semanticscholar +1 more source

