Function of mORF1 Protein as a Terminal Recognition Factor for the Linear Mitochondrial Plasmid pMLP1 from Pleurotus ostreatus

Eun Kyoung Kim, Jung Hye Roe

Research output: Contribution to journalArticlepeer-review

Abstract

The mitochondrial plasmid pMLP1 from a white-rot fungus, Pleurotus ostreatus, is a double-stranded DNA containing 381 bp terminal inverted repeat (TIR) whose 5′-ends are covalently bound by terminal proteins. The plasmid contains two major open reading frames (ORFs), encoding putative DNA and RNA polymerases, and a minor ORF encoding a small, highly basic protein. To identify the DNA binding activity that recognizes the TIR region of pMLP1, gel retardation assays were performed with mitochondrial extracts. A specific protein binding to a region between 123 and 248 nt within TIR was observed. We examined whether the gene product of mORF1 binds to this region specifically. E. coli cell extract which contains an overproduced mORF1 protein formed a complex specific to the region between 123 and 248 nt. Inclusion of mORF1 protein in the specific complex formed between P. ostreatus mitochondrial extract and TIR was confirmed by a supershift assay using polyclonal antibodies against the mORF1 protein. Our result suggests that the product of mORF1 may function as a terminal region recognition factor (TRF), recognizing an internal region in TIR.

Original languageEnglish (US)
Pages (from-to)229-233
Number of pages5
JournalJournal of Microbiology
Volume37
Issue number4
StatePublished - 1999
Externally publishedYes

Keywords

  • Linear mitochondrial plasmid
  • Pleurotus ostreatus
  • Pmlp1
  • Terminal inverted repeat (TIR)
  • Terminal protein
  • Terminal recognition factor

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Microbiology

Fingerprint Dive into the research topics of 'Function of mORF1 Protein as a Terminal Recognition Factor for the Linear Mitochondrial Plasmid pMLP1 from Pleurotus ostreatus'. Together they form a unique fingerprint.

Cite this