Conformation and domain structure of the non‐histone chromosomal proteins HMG 1 and 2
- 1 September 1984
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 143 (2), 323-330
- https://doi.org/10.1111/j.1432-1033.1984.tb08375.x
Abstract
The sequence of the 224 residues of HMG 1 [high mobility group 1] suggests it consists of 3 domains. The A and B domains can fold autonomously and there is also a small N domain. Several proteases are now found to cut at the end of the B domain (at or close to residue 184). The A + B-domain fragment also folds and probably contains all the helix of intact HMG 1. The stability of the B domain is enhanced by the presence of the A domain. The acidic C domain undergoes a coil .fwdarw. helix transition on lowering the pH. Several peptides were prepared by clevage at Trp. Peptide 57-C-terminus contains complete B and C domains but does not fold. In the absence of the A domain the C domain is thus able to destabilize the B domain. The stability of the B domain in HMG 1 is due to interaction with the A domain and the C domain has a separate function from the other domains.This publication has 25 references indexed in Scilit:
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