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Plant Cell, Vol. 12, 991-1002, June 2000, Copyright © 2000, American Society of Plant Physiologists

Arabidopsis MutS Homologs—AtMSH2, AtMSH3, AtMSH6, and a Novel AtMSH7—Form Three Distinct Protein Heterodimers with Different Specificities for Mismatched DNA

Kevin M. Culligana and John B. Haysb
a Program in Molecular and Cellular Biology, Oregon State University, Corvallis, Oregon 97331
b Department of Environmental and Molecular Toxicology, Oregon State University, Corvallis, Oregon 97331

Correspondence to: John B. Hays, haysj{at}bcc.orst.edu (E-mail), 541-737-0497 (fax)

Arabidopsis mismatch repair genes predict MutS-like proteins remarkably similar to eukaryotic MutS homologs—MSH2, MSH3, and MSH6. A novel feature in Arabidopsis is the presence of two MSH6-like proteins, designated AtMSH6 and AtMSH7. Combinations of Arabidopsis AtMSH2 with AtMSH3, AtMSH6, or AtMSH7 proteins—products of in vitro transcription and translation—were analyzed for interactions by analytical gel filtration chromatography. The AtMSH2 protein formed heterodimers with AtMSH3, AtMSH6, and AtMSH7, but no single proteins formed homodimers. The abilities of the various heterodimers to bind to mismatched 51-mer duplexes were measured by electrophoretic mobility-shift assays. Similar to the behavior of the corresponding human proteins, AtMSH2•AtMSH3 heterodimers bound "insertion–deletion" DNA with three nucleotides (+AAG) or one nucleotide (+T) looped out much better than they bound DNA with a base/base mispair (T/G), whereas AtMSH2•AtMSH6 bound the (+T) substrate strongly, (T/G) well, and (+AAG) no better than it did a (T/A) homoduplex. However, AtMSH2•AtMSH7 showed a different specificity: moderate affinity for a (T/G) substrate and weak binding of (+T). Thus, AtMSH2•AtMSH7 may be specialized for lesions/base mispairs not tested or for (T/G) mispairs in special contexts.




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