An O6-methylguanine-DNA methyltransferase-like protein from Thermus thermophilus interacts with a nucleotide excision repair protein.

doi:10.1093/jb/mvn065

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

An O6-methylguanine-DNA methyltransferase-like protein from Thermus thermophilus interacts with a nucleotide excision repair protein.

Journal of biochemistry - 1 Aug 2008

Morita Rihito, Nakagawa Noriko, Kuramitsu Seiki, Masui Ryoji

Abstract excerpt

The major damage to DNA caused by alkylating agents involves the formation of O6-methylguanine (O6-meG). Almost all species possess O6-methylguanine-DNA-methyltransferase (Ogt) to repair such damage. Ogt repairs O6-meG lesions in DNA by stoichiometric transfer of the methyl group to a cysteine residue in its active site (PCHR). Thermus thermophilus HB8 has an Ogt homologue, TTHA1564, but in this case an alanine...

Topics

Amino Acid Sequence
Bacterial Proteins
DNA
DNA Repair
DNA Repair Enzymes
DNA-Binding Proteins
Guanine
Molecular Sequence Data
Mutation
O(6)-Methylguanine-DNA Methyltransferase
Sequence Homology, Amino Acid
Thermus thermophilus

Source

Open in PubMed

Identifiers

PMID: 18483064
DOI: 10.1093/jb/mvn065

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics