TIM10 cDNA ORF clone, Saccharomyces cerevisiae S288C

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.
Johnston M, Andrews S, Brinkman R, Cooper J, Ding H, Dover J, Du Z, Favello A, Fulton L, Gattung S
Science (New York, N.Y.)265(5181)2077-82(1994 Sep)

Tim10 is protected from degradation by the protease Yme1 by Tim9.
Title: Mitochondrial Tim9 protects Tim10 from degradation by the protease Yme1.

No individual cysteine residue is required for the function of Tim9 or Tim10 in yeast and defective assembly of the small TIMs induces their proteolytic clearance from mitochondria via the mitochondrial ATP-dependent protease, Yme1.
Title: Impaired folding of the mitochondrial small TIM chaperones induces clearance by the i-AAA protease.

A region within the Tim9 and Tim10 precursors, consisting of only nine amino acid residues, functions as a signal for the engagement of substrate proteins with the Mia40 receptor.
Title: Identification of the signal directing Tim9 and Tim10 into the intermembrane space of mitochondria.

zinc is a powerful inhibitor of Erv1, an essential component of the import pathway used by the small Tim9,10 proteins
Title: Zinc can play chaperone-like and inhibitor roles during import of mitochondrial small Tim proteins.

The structure of the yeast Tim9-Tim10 hexameric assembly determined to 2.5 A is reported and mutational analysis was performed to evaluate the specific roles of Tim9 and Tim10.
Title: Structural and functional requirements for activity of the Tim9-Tim10 complex in mitochondrial protein import.