An active second dihydrofolate reductase enzyme is not a feature of rat and mouse, but they do have activity in their mitochondria

FEBS Lett. 2015 Jul 8;589(15):1855-62. doi: 10.1016/j.febslet.2015.05.017. Epub 2015 May 14.

Abstract

The identification of a second functional dihydrofolate reductase enzyme in humans, DHFRL1, led us to consider whether this is also a feature of rodents. We demonstrate that dihydrofolate reductase activity is also a feature of the mitochondria in both rat and mouse but this is not due to a second enzyme. While our phylogenetic analysis revealed that RNA-mediated DHFR duplication events did occur across the mammal tree, the duplicates in brown rat and mouse are likely to be processed pseudogenes. Humans have evolved the need for two separate enzymes while laboratory rats and mice have just one.

Keywords: Dihydrofolate reductase; Folic acid; Mitochondria; Mouse; R. norvegicus; R. rattus; Rat.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • DNA Primers
  • Mice
  • Mitochondria / enzymology*
  • Molecular Sequence Data
  • Open Reading Frames
  • Phylogeny
  • Polymerase Chain Reaction
  • Rats
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Homology, Amino Acid
  • Tetrahydrofolate Dehydrogenase / classification
  • Tetrahydrofolate Dehydrogenase / genetics
  • Tetrahydrofolate Dehydrogenase / metabolism*

Substances

  • DNA Primers
  • Tetrahydrofolate Dehydrogenase