Endogenous epitope tagging of heat shock protein 70 isoform Hsc70 using CRISPR/Cas9.

ABSTRACT: Heat shock protein 70 (Hsp70) is an evolutionarily well-conserved molecular chaperone involved in several cellular processes such as folding of proteins, modulating protein-protein interactions, and transport of proteins across the membrane. Binding partners of Hsp70 (known as "clients") are identified on an individual basis as researchers discover their particular protein of interest binds to Hsp70. A full complement of Hsp70 interactors under multiple stress conditions remains to be determined. A promising approach to characterizing the Hsp70 "interactome" is the use of protein epitope tagging and then affinity purification followed by mass spectrometry (AP-MS/MS). AP-MS analysis is a widely used method to decipher protein-protein interaction networks and identifying protein functions. C

SUBMITTER: Nitika 

PROVIDER: S-EPMC5904078 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature