Concerted formation of macromolecular Suppressor-mutator transposition complexes

Ramesh Raina, Michael Schläppi, Balasulojini Karunanandaa, Adam Elhofy, Nina Fedoroff

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

Transposition of the maize Suppressor-mutator (Spm) transposon requires two element-encoded proteins, TnpA and TnpD. Although there are multiple TnpA binding sites near each element end, binding of TnpA to DNA is not cooperative, and the binding affinity is not markedly affected by the number of binding sites per DNA fragment. However, intermolecular complexes form cooperatively between DNA fragments with three or more TnpA binding sites. TnpD, itself not a sequence-specific DNA-binding protein, binds to TnpA and stabilizes the TnpA-DNA complex. The high redundancy of TnpA binding sites at both element ends and the protein-protein interactions between DNA-bound TnpA complexes and between these and TnpD imply a concerted transition of the element from a linear to a protein crosslinked transposition complex within a very narrow protein concentration range.

Original languageEnglish (US)
Pages (from-to)8526-8531
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume95
Issue number15
DOIs
StatePublished - Jul 21 1998
Externally publishedYes

Keywords

  • DNA-protein interaction
  • Maize
  • TnpA
  • TnpD

ASJC Scopus subject areas

  • General

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