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. 1995 Feb 25;23(4):620–627. doi: 10.1093/nar/23.4.620

Functional analysis of Gln-237 mutants of HhaI methyltransferase.

S Mi 1, D Alonso 1, R J Roberts 1
PMCID: PMC306729  PMID: 7899082

Abstract

When the HhaI (cytosine-5) methyltransferase (M.HhaI) binds DNA it causes the target cytosine to be flipped 180 degrees out of the helix. The space becomes occupied by two amino acids, Ser-87 and Gln-237, which enter the helix from opposite sides and form a hydrogen bond to each other. Gln-237 may be involved in specific sequence recognition since it forms three hydrogen bonds to the orphan guanosine, which is the partner of the target cytosine. We have prepared all 19 mutants of Gln-237 and tested their biochemical properties. We find that mutations of this residue greatly affect the stability of the M.HhaI-DNA complex without affecting the enzyme's specificity for the target sequence. Surprisingly, all mutants retain detectable levels of enzymatic activity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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