High impact information on NDUFA12

• Using whole genome subtraction of yeasts with and without a complex I to generate candidate assembly factors, we identified a paralogue (B17.2L) of the B17.2 structural subunit [1].
• In addition, a site of oxidation of tryptophan was detected in subunit B17.2 adding to the number of post-translationally modified tryptophans we have detected in complex I subunits (Taylor, S. W., Fahy, E., Murray, J., Capaldi, R. A., and Ghosh, S. S. (2003) J. Biol. Chem. 278, 19587-19590) [2].
• One of these, a duplication of N7BM (B17.2), is particularly interesting as it has been lost from genomes that have also lost Complex I proteins, making it a candidate for a Complex I interacting protein [3].
• Although CAM 5.2 and CY-90 detected RPE cells strongly and quantitatively, clones CK5, KS-B17.2, and pancytokeratin antibody lu-5 reacted weakly and did not label some specimens [4].
• 2. Bands corresponding to cytokeratin 18 and cytokeratins 18 and 8 were seen on Western blot immunoanalysis using antibodies KS-B17.2 and CAM 5 [5].

Other interactions of NDUFA12

• AE1 and KS- B17.2 specifically labelled small cells scattered in the filament and lamellar epithelia, which are tentatively identified as neuroendocrine cells [6].
• 13; antibody KS-2.1, which is an anti-cytokeratin reacting with pseudostratified transitional and some simple epithelia; and antibody KS-B17.2 reacting with cytokeratin polypeptide no [7].

References