1y8m

From Proteopedia

Revision as of 04:30, 21 November 2007

Solution Structure of Yeast Mitochondria Fission Protein Fis1

Overview

Mitochondrial fission is facilitated by a multiprotein complex assembled, at the division site. The required components of the fission machinery in, Saccharomyces cerevisiae include Dnm1, Fis1, and Mdv1. In the present, study, we determined the protein structure of yeast Fis1 using NMR, spectroscopy. Although the six alpha-helices, as well as their folding, in, the yeast Fis1 structure are similar to those of the tetratricopeptide, repeat (TPR) domains of the human Fis1 structure, the two structures, differ in their N termini. The N-terminal tail of human Fis1 is flexible, and unstructured, whereas a major segment of the longer N terminus of, yeast Fis1 is fixed to the concave face formed by the six alpha-helices in, the TPR domains. To investigate the role of the fixed N terminus, exogenous Fis1 was expressed in yeast lacking the endogenous protein., Expression of yeast Fis1 protein rescued mitochondrial fission in delta, fis1 yeast only when the N-terminal TPR binding segment was left intact., The presence of this segment is also correlated to the recruitment of Mdv1, to mitochondria. The conformation of the N-terminal segment embedded in, the TPR pocket indicates an intra-molecular regulation of Fis1, bioactivity. Although the TPR-like helix bundle of Fis1 mediates the, interaction with Dnm1 and Mdv1, the N terminus of Fis1 is a prerequisite, to recruit Mdv1 to facilitate mitochondrial fission.

About this Structure

1Y8M is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Novel structure of the N terminus in yeast Fis1 correlates with a specialized function in mitochondrial fission., Suzuki M, Neutzner A, Tjandra N, Youle RJ, J Biol Chem. 2005 Jun 3;280(22):21444-52. Epub 2005 Apr 4. PMID:15809300

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