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Volk, David E.; Thiviyanathan, Varatharasa; House, Paul G.; Lloyd, R. Stephen; Gorenstein, David G.

doi:10.1023/a:1008386220341

Cited by 6 publications

(1 citation statement)

References 7 publications

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“…Resonance Assignments. Sequence-specific backbone resonance assignments were made by correlating cross-peaks in the HSQC, HNCO, HNCA, HN(CO)CA, HNCACB, and CBCA(CO)NH spectra in the standard manner and were reported earlier (41). The side chain resonances were determined using the 3D HCCH-TOCSY experiment.…”

Section: Resultsmentioning

confidence: 99%

Structural Similarities between MutT and the C-Terminal Domain of MutY

et al. 2000

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One of the functions of MutY from Escherchia coli is removal of adenine mispaired with 7,8-dihydro-8-oxoguanine (8-oxoG), a common lesion in oxidatively damaged DNA. MutY is composed of two domains: the larger N-terminal domain (p26) contains the catalytic properties of the enzyme while the C-terminal domain (p13) affects substrate recognition and enzyme turnover. On the basis of sequence analyses, it has been recently suggested that the C-terminal domain is distantly related to MutT, a dNTPase which hydrolyzes 8-oxo-dGTP [Noll et al. (1999) Biochemistry 38, 6374-6379]. We have studied the solution structure of the C-terminal domain of MutY by NMR and find striking similarity with the reported solution structure of MutT. Despite low sequence identity between the two proteins, they have similar secondary structure and topology. The C-terminal domain of MutY is composed of two alpha-helices and five beta-strands. The NOESY data indicate that the protein has two beta-sheets. MutT is also a mixed alpha/beta protein with two helices and two beta-sheets composed of five strands. The secondary structure elements are similarly arranged in the two proteins.

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Section: Resultsmentioning

confidence: 99%

Structural Similarities between MutT and the C-Terminal Domain of MutY

et al. 2000

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Human MutY: gene structure, protein functions and interactions, and role in carcinogenesis

Parker

Eshleman

2003

Cellular and Molecular Life Sciences (CMLS)

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Faithful maintenance of the genome is crucial to the individual and the species. Oxidative DNA damage, such as 8-oxo-7,8-dihydroguanine (8-oxoG), poses a major threat to genomic integrity. 8-OxoG can mispair with 2'-deoxycytidine 5'-triphosphate or with 2'-deoxyadenosine triphosphate during DNA replication, forming C*8-oxoG and A*8-oxoG mispairs. Human MutY is responsible for recognition and removal of the inappropriately inserted adenine in an A*8-oxoG mispair. If unrepaired, the A*8-oxoG mispairs can result in deleterious C:G to A:T transversions. Human MutY functions in a postreplication repair pathway and is targeted to the newly synthesized daughter strand of DNA for removal of the adenine base. The human MutY protein is targeted to both the mitochondria and the nucleus and associates with the proliferating cell nuclear antigen, apurinic/ apyrimidinic endonuclease 1, replication protein A and mutS homolog 6 proteins. Mutations in the human MutY gene and defective activity of the human MutY protein have been detected in cancer. A direct correlation between defective A*8-oxoG repair and increased levels of genomic 8-oxoG has now been established.

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