Description
Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.
Family
Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.
Species
Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229)
Sequence
MAEGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPENTVFDAKRLIGRRFDDESVQKDRKTWPFKLIDVEGNPVVEVQYLGETKTFSPQEISSMVLTKMKEIAEAKIGQKVEKAVITVPAYFNDAQRQATKDAGSISGLNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNMLEHFKNEFKKKTGNDISGDARALRRLRTACERAKRTLSSVTQTTIEVDSLYNGDDFETSITRARFEDLNSSLFKSTLEPVEQVLKDAKVPKTEIDEVVLVGGSTRIPKVQKMLSDFFEGKQLEKSINPDEAVAYGAAVQGAILTGQSTSEDTKDLLLLDVAPLSLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVADHQSTVQFPVYQGERVNCKENTLLGEFDLKNIPPMQAGEPVLEAIFEVDANGILKVTAVEKSTGKSANITISNAVGRLSSDEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQQVTDPVLSSKLKRGSKTKIESALSDALASLEIQDASTDDLRKAEVGLKRVVTKAMSSR
Simulated SDS-PAGE
(Note: Representative image - actual molecular weight may vary depending on tag type and expression method)
Safety
Upon ordering, we will perform rigorous biosecurity and export control screening to ensure that order fulfillment is consistent with all legal and regulatory guidance.
Protein synthesis service