Search Results - "Bochkareva, Elena S"

Evidence for a cytoplasmic pool of ribosome-free mRNAs encoding inner membrane proteins in Escherichia coli by Benhalevy, Daniel, Biran, Ido, Bochkareva, Elena S, Sorek, Rotem, Bibi, Eitan

“…Translation-independent mRNA localization represents an emerging concept in cell biology. In Escherichia coli, mRNAs encoding integral membrane proteins (MPRs)…”
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Model Uracil-Rich RNAs and Membrane Protein mRNAs Interact Specifically with Cold Shock Proteins in Escherichia coli by Benhalevy, Daniel, Bochkareva, Elena S, Biran, Ido, Bibi, Eitan

“…Are integral membrane protein-encoding mRNAs (MPRs) different from other mRNAs such as those encoding cytosolic mRNAs (CPRs)? This is implied from the emerging…”
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Membrane protein biogenesis in Ffh- or FtsY-depleted Escherichia coli by Yosef, Ido, Bochkareva, Elena S, Adler, Julia, Bibi, Eitan

“…The Escherichia coli version of the mammalian signal recognition particle (SRP) system is required for biogenesis of membrane proteins and contains two…”
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Membrane Targeting of Ribosomes and Their Release Require Distinct and Separable Functions of FtsY by Bahari, Liat, Parlitz, Richard, Eitan, Asa, Stjepanovic, Goran, Bochkareva, Elena S., Sinning, Irmgard, Bibi, Eitan

“…The mechanism underlying the interaction of the Escherichia coli signal recognition particle (SRP) receptor FtsY with the cytoplasmic membrane is not fully…”
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Escherichia coli SRP, its protein subunit Ffh, and the Ffh M domain are able to selectively limit membrane protein expression when overexpressed by Yosef, Ido, Bochkareva, Elena S, Bibi, Eitan

“…The Escherichia coli signal recognition particle (SRP) system plays an important role in membrane protein biogenesis. Previous studies have suggested…”
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New prospects in studying the bacterial signal recognition particle pathway by Herskovits, Anat A., Bochkareva, Elena S., Bibi, Eitan

“…In vivo and in vitro studies have suggested that the bacterial version of the mammalian signal recognition particle (SRP) system plays an essential and…”
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Targeting of GroEL to SecA on the Cytoplasmic Membrane of Escherichia coli by Bochkareva, Elena S., Solovieva, Maria E., Girshovich, Alexander S.

“…Chaperonin GroEL has been found to interact with isolated cytoplasmic membrane of Escherichia coli. Interaction requires Mg ions, whereas MgATP inhibits, and…”
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Putative integral membrane SRP receptors by Bibi, Eitan, Herskovits, Anat A, Bochkareva, Elena S, Zelazny, Adrian

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Evidence for coupling of membrane targeting and function of the signal recognition particle (SRP) receptor FtsY by Herskovits, Anat A, Seluanov, Andrei, Rajsbaum, Ricardo, ten Hagen-Jongman, Corinne M, Henrichs, Tanja, Bochkareva, Elena S, Phillips, Gregory J, Probst, Francis J, Nakae, Taiji, Ehrmann, Michael, Luirink, Joen, Bibi, Eitan

“…Recent studies have indicated that FtsY, the signal recognition particle receptor of Escherichia coli, plays a central role in membrane protein biogenesis. For…”
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Mutation Ala2-->Ser destabilizes intersubunit interactions in the molecular chaperone GroEL by Horovitz, A, Bochkareva, E S, Kovalenko, O, Girshovich, A S

“…The mutation Ala2-->Ser in the molecular chaperone GroEL increases positive co-operativity in ATP hydrolysis, as reflected by a change in the Hill coefficient…”
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Identification and characterization of the Escherichia coli stress protein UP12, a putative in vivo substrate of GroEL by Bochkareva, Elena S., Girshovich, Alexander S., Bibi, Eitan

“…Many groups of proteins play important roles in the cell's response to various stresses. The molecular chaperone GroEL of Escherichia coli represents one such…”
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Model Uracil-Rich RNAs and Membrane Protein mRNAs Interact Specifically with Cold Shock Proteins in Escherichia coli: e0134413 by Benhalevy, Daniel, Bochkareva, Elena S, Biran, Ido, Bibi, Eitan

“…Are integral membrane protein-encoding mRNAs (MPRs) different from other mRNAs such as those encoding cytosolic mRNAs (CPRs)? This is implied from the emerging…”
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New prospects in studying the bacterial signal recognition particle pathway: MicroReview by Herskovits, Anat A., Bochkareva, Elena S., Bibi, Eitan

“…In vivo and in vitro studies have suggested that the bacterial version of the mammalian signal recognition particle (SRP) system plays an essential and…”
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A photoactivated analog of streptomycin by Girshovich, A S, Bochkareva, E S, Ovchinnikov, Y A

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Positive cooperativity in the functioning of molecular chaperone GroEL by Bochkareva, E S, Lissin, N M, Flynn, G C, Rothman, J E, Girshovich, A S

“…In the presence of its partner, GroES, the tetradecameric molecular chaperone GroEL binds 14 ATP molecules, half of which are hydrolyzed in a cooperative…”
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ATP induces non-identity of two rings in chaperonin GroEL by Bochkareva, E S, Girshovich, A S

“…For its function, the Escherichia coli chaperonin GroEL requires the presence of ATP and co-chaperonin GroES. We have observed that ADP displays a two-step…”
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Prediction of an inter-residue interaction in the chaperonin GroEL from multiple sequence alignment is confirmed by double-mutant cycle analysis by Horovitz, A, Bochkareva, E S, Yifrach, O, Girshovich, A S

“…A search for co-ordinated amino acid changes in the hsp60 family of chaperonins suggested that cysteine residues at positions 137 and 518 in the Escherichia…”
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On the distribution of ligands within the asymmetric chaperonin complex, GroEL14 · ADP7 · GroES7 by Girshovich, Alexander S., Bochkareva, Elena S., Todd, Matthew J., Lorimer, George H.

“…In the presence of MgATP or MgADP the E. coli chaperonin proteins, GroEL and GroES, form a stable asymmetric complex with a stoichiometry of two GroEL7:one…”
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The N terminus of the molecular chaperonin GroEL is a crucial structural element for its assembly by Horovitz, A., Bochkareva, E.S., Girshovich, A.S.

“…The Escherichia coli heat-shock protein GroEL is a member of the highly conserved family of tetradecameric chaperonins 60, which assist in the folding and…”
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On the distribution of ligands within the asymmetric chaperonin complex, GroEL 14 · ADP 7 · GroES 7 by Girshovich, Alexander S., Bochkareva, Elena S., Todd, Matthew J., Lorimer, George H.

“…In the presence of MgATP or MgADP the E. coli chaperonin proteins, GroEL and GroES, form a stable asymmetric complex with a stoichiometry of two GroEL 7:one…”
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