GROEL ES-MEDIATED REFOLDING OF HUMAN CARBONIC-ANHYDRASE-II - ROLE OF N-TERMINAL HELICES AS RECOGNITION MOTIFS FOR GROEL/

The presence of GroEL/ES during the refolding of human carbonic anhydr ase II (pseudo-wild type) was found to increase the yield of active en zyme from 65 to 100%. This chaperone action on the enzyme could be obt ained by adding GroEL alone, and the time-course in that case was only moderately slower than the spontaneous process. Truncated forms of ca rbonic anhydrase, in which N-terminal helices were removed, also serve d as protein substrates for GroEL/ES. This demonstrates that N-termina lly located helices are not obligatory as recognition motifs.