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Gene Review:

JAC1 - Jac1p

Saccharomyces cerevisiae S288c

Synonyms: J-type accessory chaperone 1, J-type co-chaperone JAC1, mitochondrial, SEO2, YGL018C

Strain, J. et al., Huynen, M.A. et al., Andrew, A.J. et al., Kim, R. et al., Voisine, C. et al., et al.

Huynen, Snel, Bork, Gibson,

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High impact information on JAC1

Fe/S enzyme activities remain low in both jac1 and ssq1 mutant mitochondria even if normal mitochondrial iron levels are maintained [1].
Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae [1].
JAC1, an ortholog of hscB, and SSQ1, a paralog of hscA, have been shown to be required for iron-sulfur cluster assembly in mitochondria of Saccharomyces cerevisiae [2].
In 56 available genomes we identified two genes with identical phylogenetic distributions to the frataxin/cyaY gene: hscA and hscB/JAC1 [2].
Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p [3].

Biological context of JAC1

A second sod1Delta suppressor gene, designated JAC1, represents a new member of the 20-kDa J-protein family of co-chaperones [4].
Jac1p contains a mitochondrial targeting consensus sequence and may serve as the partner for Ssq1p [4].
Homologues of Ssq1p and Jac1p are found in bacteria in close association with genes proposed to be involved in iron-sulfur protein biosynthesis [4].
Jac1p is a conserved, specialized J-protein that functions with Hsp70 in Fe-S cluster biogenesis in mitochondria of the yeast Saccharomyces cerevisiae [3].
Similar mitochondrial localization and similar mutant phenotypes suggest that Ssq1p and Jac1p are functional partners in iron homeostasis [5].

Other interactions of JAC1

Taken together these results suggest a role for Ssq1p, Jac1p, and Nfs1p in assembly/maturation of mitochondrial iron-sulfur proteins and that one or more of the target Fe/S proteins contribute to oxidative damage in cells lacking copper/zinc SOD [4].
In jac1 mutants, like in ssq1 mutants, processing of the Yfh1p precursor protein from intermediate to mature forms was delayed [5].
Taken together, these data suggest that Ssq1p/Jac1p/Mge1p are not important for Fe/S cluster synthesis on Isu1p [6].
The mitochondrial DnaJ homolog Jac1 is crucial for this process, whereas Mdj1 function is dispensable [7].

References

Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae. Voisine, C., Cheng, Y.C., Ohlson, M., Schilke, B., Hoff, K., Beinert, H., Marszalek, J., Craig, E.A. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly. Huynen, M.A., Snel, B., Bork, P., Gibson, T.J. Hum. Mol. Genet. (2001) [Pubmed]
Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p. Andrew, A.J., Dutkiewicz, R., Knieszner, H., Craig, E.A., Marszalek, J. J. Biol. Chem. (2006) [Pubmed]
Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly. Strain, J., Lorenz, C.R., Bode, J., Garland, S., Smolen, G.A., Ta, D.T., Vickery, L.E., Culotta, V.C. J. Biol. Chem. (1998) [Pubmed]
J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins. Kim, R., Saxena, S., Gordon, D.M., Pain, D., Dancis, A. J. Biol. Chem. (2001) [Pubmed]
The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p. Dutkiewicz, R., Marszalek, J., Schilke, B., Craig, E.A., Lill, R., Mühlenhoff, U. J. Biol. Chem. (2006) [Pubmed]
The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria. Lutz, T., Westermann, B., Neupert, W., Herrmann, J.M. J. Mol. Biol. (2001) [Pubmed]

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AGOS_AGR164C	Ashbya gossypii ATCC 10895
KLLA0A04840g	Kluyveromyces lactis NRRL Y-1140
MGG_14699	Magnaporthe oryzae 70-15
NCU07360	Neurospora crassa OR74A

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