Abstract

Summary: Mitochondrial DNA(mtDNA)is packed into highly organized structures called mitochondrial nucleoids(mt-nucleoids). We identified and characterized a new mitochondrial histone-like protein, termed Glom(a protein inducing agglomeration of mitochondrial chromosome), from highly condensed mt-nucleoids of the true slime mold, Physarum polycephalum. This protein has a lysine-rich region with proline-rich domain in the N-terminal half and two HMG boxes in C-terminal half. Glom induced intensive DNA condensation without suppressing replication and transcription. The lysine-rich region was sufficient for the mtDNA condensation and the proline-rich domain was essential to keep those genetic activities. The expression of Glom also complemented the E.coli mutant lacking the bacterial histone-like protein HU and the HMG-boxes region of Glom was important for the complementation.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.