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The C6 zinc cluster dictates asymmetric binding by HAP1.
Author(s) -
Zhang L.,
Guarente L.
Publication year - 1996
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1996.tb00844.x
Subject(s) - biology , cluster (spacecraft) , zinc , computational biology , evolutionary biology , materials science , computer science , metallurgy , programming language
Unlike other C6 zinc cluster proteins such as GAL4 and PPR1, HAP1 binds selectively to asymmetric DNA sites containing a direct repeat of two CGG triplets. Here, we show that the HAP1 zinc cluster is solely responsible for asymmetric binding by HAP1. An asymmetric interaction between two zinc clusters of a HAP1 dimer must position the zinc clusters in a directly repeated orientation, and enable them to recognize two CGG triplets in a direct repeat. Further, our data suggest that this asymmetric interaction acts cooperatively with the interaction between dimerization elements to promote HAP1 dimerization, and locks HAP1‐DNA complexes in a stable, dimeric conformation.