Protein binding to a single termination-associated sequence in the mitochondrial DNA D-loop region.

We identified a single protected sequence element located 58 bases upstream from the D-loop 3' end

C S Madsen


Scholarcy highlights

  • A methylation protection assay was used in a novel manner to demonstrate a specific bovine proteinmitochondrial DNA interaction within the organelle
  • We have identified a candidate bovine mitochondrial protein(s) that binds to a sequence element which is evolutionally conserved among vertebrates
  • MtDNA replication begins at the origin of H-strand synthesis, whether or not this initial synthesis event results in the production of an H-strand D-loop DNA or a complete mitochondrial genome is thought to be governed by a termination mechanism likely to involve termination-associated sequence elements
  • As a precedent for this type of mechanism, Escherichia coli leading-strand DNA synthesis is terminated in a sequence-specific manner in vitro through binding of TUS protein factor
  • In view of the fact that a footprint is seen in mitochondria from brain cortex tissue, it is reasonable to assume that a relatively high proportion of the TAS-A sites in the mitochondria are occupied by protein
  • High TAS occupancy in conjunction with rapid D-loop turnover and abundance of D-loop mitochondrial forms in highly oxidative tissues favor a mechanism in which protein binding to TAS leads to the early termination of H-strand replication and creation of D-loop strands; that is, these data favor the view that TAS-A binding is a negative regulator of H-strand
  • Under certain conditions, such as actively dividing mammalian cells in culture, in which initiation of H-strand DNA synthesis appears to be almost constitutive , producing a complete mitochondrial genome may be predominately regulated by the presence or absence of termination-associated sequence binding

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