MutSα mismatch repair protein stability is governed by subunit interaction, acetylation, and ubiquitination.

Tim Arlow¹, Junwon Kim², Joanna E Haye-Bertolozzi³, Cristina Balbás Martínez⁴, Caitlin Fay⁵, Emma Zorensky⁶, Mark D Rose⁷, Alison E Gammie⁸

¹Ophthalmic Associates, Johnstown, PA.

²Deceased.

³Xavier University of Louisiana, New Orleans, LA.

⁴Escuelab, Madrid, Community of Madrid, Spain.

⁵Tufts Medical Center, Boston, MA 02118.

⁶Sempre Health, San Francisco, CA.

⁷Georgetown University, Georgetown, Washington D.C.

⁸National Institute of General Medical Sciences, Bethesda, MD.

PubMed PMC DOI PDF

Abstract

In eukaryotes, DNA mismatch recognition is accomplished by the highly conserved MutSα (Msh2/Msh6) and MutSβ (Msh2/Msh3) complexes. Previously, in the yeast Saccharomyces cerevisiae, we determined that deleting MSH6 caused wild-type Msh2 levels to drop by ∼50%. In this work, we determined that Msh6 steady-state levels are coupled to increasing or decreasing levels of Msh2. Although Msh6 and Msh2 ar…

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