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MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III

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Michaels, Mark Leo, Pham, Lucie, Nghiem, Ylan, Cruz, Christina, Miller, Jeffrey H.·1990·Nucleic Acids Research

Abstract

The mutY gene of Escherichia coli, which codes for an adenine glycosylase that excises the adenine of a G-A mispair, has been cloned and sequenced. The mutY gene codes for a protein of 350 amino acids (Mr = 39,123) and the clone genetically complements the mutY strain. The protein shows significant sequence homology to E. coli endonuclease III, an enzyme that has previously been shown to have glycosylase activity on damaged base pairs. Sequence analysis suggests that, like endonuclease III, MutY is an iron-sulfur protein with a [4Fe-4S]2+ cluster.

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Metadata

Authors
Michaels, M. L., Pham, L., Nghiem, Y., Cruz, C., & Miller, J. H.
Venue
Nucleic Acids Research
Published
1990
Volume
18
Issue
13
Pages
3841-3845
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
OpenAlex
W2040358738
Cited by
179
References
0
FWCI
2.97
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III. https://app.cochat.ai/papers/10.1093/nar/18.13.3841
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Michaels, M. L., Pham, L., Nghiem, Y., Cruz, C., & Miller, J. H. (1990). MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III. Nucleic Acids Research. https://doi.org/10.1093/nar/18.13.3841

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