Abstract:
:Three homologous aspartate aminotransferases with virtually identical spatial structures and pairwise amino acid sequence identities of > 40% differ markedly with respect to the yield of renaturation upon dilution from 6 M guanidine hydrochloride (mitochondrial < cytosolic < Escherichia coli). The enzymes also respond differently to molecular chaperones. GroEL/GroES, the Hsp60 homolog of E. coli, increased considerably the yield of renaturation of mitochondrial aspartate aminotransferase and to a lesser extent that of its cytosolic counterpart, but not that of the E. coli enzyme. DnaK/DnaJ/GrpE, the Hsp70 system of E. coli, also increased the yield of renaturation of mitochondrial aspartate aminotransferase. Apparently, specific features in the amino acid sequence or the folding pathway which are independent of the final secondary and tertiary structure determine the interactions of the folding proteins with the chaperone systems.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Widmann M,Christen Pdoi
10.1016/0014-5793(95)01406-3subject
Has Abstractpub_date
1995-12-27 00:00:00pages
481-4issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(95)01406-3journal_volume
377pub_type
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