Journal article

Conserved motifs reveal details of ancestry and structure in the small TIM chaperones of the mitochondrial intermembrane space

Ian E Gentle, Andrew J Perry, Felicity H Alcock, Vladimir A Likic, Pavel Dolezal, Ee Ting Ng, Anthony W Purcell, Malcolm McConnville, Thomas Naderer, Anne-Laure Chanez, Fabien Charriere, Caroline Aschinger, Andre Schneider, Kostas Tokatlidis, Trevor Lithgow

MOLECULAR BIOLOGY AND EVOLUTION | OXFORD UNIV PRESS | Published : 2007

Abstract

The mitochondrial inner and outer membranes are composed of a variety of integral membrane proteins, assembled into the membranes posttranslationally. The small translocase of the inner mitochondrial membranes (TIMs) are a group of approximately 10 kDa proteins that function as chaperones to ferry the imported proteins across the mitochondrial intermembrane space to the outer and inner membranes. In yeast, there are 5 small TIM proteins: Tim8, Tim9, Tim10, Tim12, and Tim13, with equivalent proteins reported in humans. Using hidden Markov models, we find that many eukaryotes have proteins equivalent to the Tim8 and Tim13 and the Tim9 and Tim10 subunits. Some eukaryotes provide "snapshots" of ..

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