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P11484
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Ribosome-associated molecular chaperone SSB1 |
Ribosome-bound, Hsp70-type chaperone that assists in thecotranslational folding of newly synthesized proteins in the cytosol.Stimulates folding by interacting with nascent chains, binding toshort, largely hydrophobic sequences exposed by unfolded proteins,thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably untilfully synthesized. The Hsp70-protein substrate interaction depends onATP-binding and on allosteric regulation between the NBD and the SBD.The ATP-bound state is characterized by a fast exchange rate ofsubstrate (low affinity state), while in the ADP-bound state exchangeis much slower (high affinity state). During the Hsp70 cycle, thechaperone switches between the ATP-bound state (open conformation) andthe ADP-bound state (closed conformation) by major conformationalrearrangements involving mainly the lid domain. Ssb cooperates with aspecific Hsp40/Hsp70 co-chaperone termed the ribosome-associatedcomplex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substratebinding state. Hsp110 chaperone SSE1 and FES1 act as nucleotideexchange factors that cause substrate release |
YDL229W |
Saccharomyces cerevisiae |
RSY113 |
20559436
|
|
P11484
|
Ribosome-associated molecular chaperone SSB1 |
Ribosome-bound, Hsp70-type chaperone that assists in thecotranslational folding of newly synthesized proteins in the cytosol.Stimulates folding by interacting with nascent chains, binding toshort, largely hydrophobic sequences exposed by unfolded proteins,thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably untilfully synthesized. The Hsp70-protein substrate interaction depends onATP-binding and on allosteric regulation between the NBD and the SBD.The ATP-bound state is characterized by a fast exchange rate ofsubstrate (low affinity state), while in the ADP-bound state exchangeis much slower (high affinity state). During the Hsp70 cycle, thechaperone switches between the ATP-bound state (open conformation) andthe ADP-bound state (closed conformation) by major conformationalrearrangements involving mainly the lid domain. Ssb cooperates with aspecific Hsp40/Hsp70 co-chaperone termed the ribosome-associatedcomplex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substratebinding state. Hsp110 chaperone SSE1 and FES1 act as nucleotideexchange factors that cause substrate release |
YDL229W |
Saccharomyces cerevisiae |
RSY255 |
20559436
|
|
P11484
|
Ribosome-associated molecular chaperone SSB1 |
Ribosome-bound, Hsp70-type chaperone that assists in thecotranslational folding of newly synthesized proteins in the cytosol.Stimulates folding by interacting with nascent chains, binding toshort, largely hydrophobic sequences exposed by unfolded proteins,thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably untilfully synthesized. The Hsp70-protein substrate interaction depends onATP-binding and on allosteric regulation between the NBD and the SBD.The ATP-bound state is characterized by a fast exchange rate ofsubstrate (low affinity state), while in the ADP-bound state exchangeis much slower (high affinity state). During the Hsp70 cycle, thechaperone switches between the ATP-bound state (open conformation) andthe ADP-bound state (closed conformation) by major conformationalrearrangements involving mainly the lid domain. Ssb cooperates with aspecific Hsp40/Hsp70 co-chaperone termed the ribosome-associatedcomplex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substratebinding state. Hsp110 chaperone SSE1 and FES1 act as nucleotideexchange factors that cause substrate release |
YDL229W |
Saccharomyces cerevisiae |
RSY782 |
20559436
|
|
P11484
|
Ribosome-associated molecular chaperone SSB1 |
Ribosome-bound, Hsp70-type chaperone that assists in thecotranslational folding of newly synthesized proteins in the cytosol.Stimulates folding by interacting with nascent chains, binding toshort, largely hydrophobic sequences exposed by unfolded proteins,thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably untilfully synthesized. The Hsp70-protein substrate interaction depends onATP-binding and on allosteric regulation between the NBD and the SBD.The ATP-bound state is characterized by a fast exchange rate ofsubstrate (low affinity state), while in the ADP-bound state exchangeis much slower (high affinity state). During the Hsp70 cycle, thechaperone switches between the ATP-bound state (open conformation) andthe ADP-bound state (closed conformation) by major conformationalrearrangements involving mainly the lid domain. Ssb cooperates with aspecific Hsp40/Hsp70 co-chaperone termed the ribosome-associatedcomplex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substratebinding state. Hsp110 chaperone SSE1 and FES1 act as nucleotideexchange factors that cause substrate release |
YDL229W |
Saccharomyces cerevisiae |
RSY954 |
20559436
|
|
P11484
|
Ribosome-associated molecular chaperone SSB1 |
Ribosome-bound, Hsp70-type chaperone that assists in thecotranslational folding of newly synthesized proteins in the cytosol.Stimulates folding by interacting with nascent chains, binding toshort, largely hydrophobic sequences exposed by unfolded proteins,thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably untilfully synthesized. The Hsp70-protein substrate interaction depends onATP-binding and on allosteric regulation between the NBD and the SBD.The ATP-bound state is characterized by a fast exchange rate ofsubstrate (low affinity state), while in the ADP-bound state exchangeis much slower (high affinity state). During the Hsp70 cycle, thechaperone switches between the ATP-bound state (open conformation) andthe ADP-bound state (closed conformation) by major conformationalrearrangements involving mainly the lid domain. Ssb cooperates with aspecific Hsp40/Hsp70 co-chaperone termed the ribosome-associatedcomplex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substratebinding state. Hsp110 chaperone SSE1 and FES1 act as nucleotideexchange factors that cause substrate release |
YDL229W |
Saccharomyces cerevisiae |
SEY6210 |
20559436
|
|
P11484
|
Ribosome-associated molecular chaperone SSB1 |
Ribosome-bound, Hsp70-type chaperone that assists in thecotranslational folding of newly synthesized proteins in the cytosol.Stimulates folding by interacting with nascent chains, binding toshort, largely hydrophobic sequences exposed by unfolded proteins,thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably untilfully synthesized. The Hsp70-protein substrate interaction depends onATP-binding and on allosteric regulation between the NBD and the SBD.The ATP-bound state is characterized by a fast exchange rate ofsubstrate (low affinity state), while in the ADP-bound state exchangeis much slower (high affinity state). During the Hsp70 cycle, thechaperone switches between the ATP-bound state (open conformation) andthe ADP-bound state (closed conformation) by major conformationalrearrangements involving mainly the lid domain. Ssb cooperates with aspecific Hsp40/Hsp70 co-chaperone termed the ribosome-associatedcomplex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substratebinding state. Hsp110 chaperone SSE1 and FES1 act as nucleotideexchange factors that cause substrate release |
YDL229W |
Saccharomyces cerevisiae |
SF264-1D |
20559436
|
|
P11484
|
Ribosome-associated molecular chaperone SSB1 |
Ribosome-bound, Hsp70-type chaperone that assists in thecotranslational folding of newly synthesized proteins in the cytosol.Stimulates folding by interacting with nascent chains, binding toshort, largely hydrophobic sequences exposed by unfolded proteins,thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably untilfully synthesized. The Hsp70-protein substrate interaction depends onATP-binding and on allosteric regulation between the NBD and the SBD.The ATP-bound state is characterized by a fast exchange rate ofsubstrate (low affinity state), while in the ADP-bound state exchangeis much slower (high affinity state). During the Hsp70 cycle, thechaperone switches between the ATP-bound state (open conformation) andthe ADP-bound state (closed conformation) by major conformationalrearrangements involving mainly the lid domain. Ssb cooperates with aspecific Hsp40/Hsp70 co-chaperone termed the ribosome-associatedcomplex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substratebinding state. Hsp110 chaperone SSE1 and FES1 act as nucleotideexchange factors that cause substrate release |
YDL229W |
Saccharomyces cerevisiae |
Snf7 |
20559436
|
|
P11484
|
Ribosome-associated molecular chaperone SSB1 |
Ribosome-bound, Hsp70-type chaperone that assists in thecotranslational folding of newly synthesized proteins in the cytosol.Stimulates folding by interacting with nascent chains, binding toshort, largely hydrophobic sequences exposed by unfolded proteins,thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably untilfully synthesized. The Hsp70-protein substrate interaction depends onATP-binding and on allosteric regulation between the NBD and the SBD.The ATP-bound state is characterized by a fast exchange rate ofsubstrate (low affinity state), while in the ADP-bound state exchangeis much slower (high affinity state). During the Hsp70 cycle, thechaperone switches between the ATP-bound state (open conformation) andthe ADP-bound state (closed conformation) by major conformationalrearrangements involving mainly the lid domain. Ssb cooperates with aspecific Hsp40/Hsp70 co-chaperone termed the ribosome-associatedcomplex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substratebinding state. Hsp110 chaperone SSE1 and FES1 act as nucleotideexchange factors that cause substrate release |
YDL229W |
Saccharomyces cerevisiae |
VPS23 |
20559436
|