Journal article

Patterns that define the four domains conserved in known and novel isoforms of the protein import receptor Tom20

VA Likić, A Perry, J Hulett, M Derby, A Traven, RF Waller, PJ Keeling, CM Koehler, SP Curran, PR Gooley, T Lithgow

Journal of Molecular Biology | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | Published : 2005

Abstract

Tom20 is the master receptor for protein import into mitochondria. Analysis of motifs present in Tom20 sequences from fungi and animals found several highly conserved regions, including features of the transmembrane segment, the ligand-binding domain and functionally important flexible segments at the N terminus and the C terminus of the protein. Hidden Markov model searches of genome sequence data revealed novel isoforms of Tom20 in vertebrate and invertebrate animals. A three-dimensional comparative model of the novel type I Tom20, based on the structurally characterized type II isoform, shows important differences in the amino acid residues lining the ligand-binding groove, where the type..

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University of Melbourne Researchers