Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
ATP12 family protein
Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesised as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment [3]. These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly. [1]. 2142305. Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase. Ackerman SH, Tzagoloff A;. Proc Natl Acad Sci U S A 1990;87:4986-4990. [2]. 10747017. The alpha-subunit of the mitochondrial F(1) ATPase interacts directly with the assembly factor Atp12p. Wang ZG, Sheluho D, Gatti DL, Ackerman SH;. EMBO J 2000;19:1486-1493. [3]. 1826907. Characterization of ATP12, a yeast nuclear gene required for the assembly of the mitochondrial F1-ATPase. Bowman S, Ackerman SH, Griffiths DE, Tzagoloff A;. J Biol Chem 1991;266:7517-7523. (from Pfam)
ATP12 family chaperone protein
ATP12 family chaperone protein similar to Homo sapiens ATP synthase mitochondrial F1 complex assembly factor 2 that may play a role in the assembly of the F1 component of the mitochondrial ATP synthase (ATPase), as well as to Saccharomyces cerevisiae mitochondrial protein ATP12, which is essential for the assembly of the mitochondrial F1-F0 complex
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on