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Chung Wang

Publications and source records attributed to Chung Wang.

4 recordsLinked to original sources
PubMed2005

Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions.

Previously, we identified the human small glutamine-rich tetratricopeptide repeat-containing protein (SGT) as a co-chaperone. The tetratricopeptide repeat (TPR) domain in SGT is responsible for interacting with Hsc70. In this study, we demonstrated that the TPR domain of SGT also interacted with Hsp90. Moreover, we investigated the functional significance of regions of SGT outside the TPR domain. Evidently, the N-terminal domain of SGT is necessary and sufficient for its self-association; and, SGT may be a dimer elongated in shape. The C-terminal glutamine-rich region has the capacity to interact with short peptide segments composed of consecutive non-polar amino acids. The C-terminal fragment of SGT indeed plays a role in the association of SGT with in vitro translated rat type 1 glucose transporter, an integral membrane protein folded in a non-physiological state. Moreover, in the presence of SGT, the degradation of the transporter in reticulocyte lysates is inhibited. Taking together, SGT can be separated into three structural units with distinct functions.

Animals↗
PubMed2003

Crystal structure of the C-terminal 10-kDa subdomain of Hsc70.

The 70-kDa heat shock proteins (Hsp70), including the cognates (Hsc70), are molecular chaperones that prevent misfolding and aggregation of polypeptides in cells under both normal and stressed conditions. They are composed of two major structural domains: an N-terminal 44-kDa ATPase domain and a C-terminal 30-kDa substrate binding domain. The 30-kDa domain can be divided into an 18-kDa subdomain and a 10-kDa subdomain. Here we report the crystal structure of the 10-kDa subdomain of rat Hsc70 at 3.45 A. Its helical region adopted a helix-loop-helix fold. This conformation is different from the equivalent subdomain of DnaK, the bacterial homologue of Hsc70. Moreover, in the crystalline state, the 10-kDa subdomain formed dimers. The results of gel filtration chromatography further supported the view that this subdomain was self-associated. Upon gel filtration, Hsc70 was found to exist as a mixture of monomers, dimers, and oligomers, but the 60-kDa fragment was predominantly found to exist as monomers. These findings suggest that the alpha-helical region of the 10-kDa subdomain dictates the chaperone self-association.

Amino Acid Sequence↗
PubMed2002

Characterization of the L399P and R447G mutants of hsc70: the decrease in refolding activity is correlated with an increase in the rate of substrate dissociation.

It is known that 70-kDa heat-shock cognate protein (hsc70) is capable of forming complexes with unfolded polypeptide substrates and works with DnaJ homologues to refold denatured proteins. Herein, we characterized two hsc70 mutants, hsc70(L399P) and hsc70(R447G). They retained the capability of restoring the activity of denatured luciferase, but their activity was decreased to 40% and 20%, respectively, of that of hsc70. The rate of dissociation for the heptapeptide substrate FYQLALT from the mutants was increased, and the R447G mutant had the faster rate of peptide dissociation. Thus, the reduction in the ability of these mutants to refold denatured proteins was correlated with an increase in the rate of substrate dissociation.

HSP40 Heat-Shock Proteins↗