A stable tetramer is not the only oligomeric state that mitochondrial single-stranded DNA binding proteins can adopt.

ABSTRACT: Mitochondrial single-stranded DNA (ssDNA)-binding proteins (mtSSBs) are required for mitochondrial DNA replication and stability and are generally assumed to form homotetramers, and this species is proposed to be the one active for ssDNA binding. However, we recently reported that the mtSSB from Saccharomyces cerevisiae (ScRim1) forms homotetramers at high protein concentrations, whereas at low protein concentrations, it dissociates into dimers that bind ssDNA with high affinity. In this work, using a combination of analytical ultracentrifugation techniques and DNA binding experiments with fluorescently labeled DNA oligonucleotides, we tested whether the ability of ScRim1 to form dimers is unique among mtSSBs. Although human mtSSBs and those from Schizosaccharomyces

SUBMITTER: Singh SP 

PROVIDER: S-EPMC6422086 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature