RRC ID 30227
著者 Müller C, Maeso I, Wittbrodt J, Martínez-Morales JR.
タイトル The medaka mutation tintachina sheds light on the evolution of V-ATPase B subunits in vertebrates.
ジャーナル Sci Rep
Abstract Vacuolar-type H(+) ATPases (V-ATPases) are multimeric protein complexes that play a universal role in the acidification of intracellular compartments in eukaryotic cells. We have isolated the recessive medaka mutation tintachina (tch), which carries an inactivating modification of the conserved glycine residue (G75R) of the proton pump subunit atp6v1Ba/vatB1. Mutant embryos show penetrant pigmentation defects, massive brain apoptosis and lethality before hatching. Strikingly, an equivalent mutation in atp6v1B1 (G78R) has been reported in a family of patients suffering from distal renal tubular acidosis (dRTA), a hereditary disease that causes metabolic acidosis due to impaired kidney function. This poses the question as to how molecularly identical mutations result in markedly different phenotypes in two vertebrate species. Our work offers an explanation for this phenomenon. We propose that, after successive rounds of whole-genome duplication, the emergence of paralogous copies allowed the divergence of the atp6v1B cis-regulatory control in different vertebrate groups.
巻・号 3
ページ 3217
公開日 2013-11-14
DOI 10.1038/srep03217
PII srep03217
PMID 24225653
PMC PMC3827601
MeSH Animals Biological Evolution Molecular Sequence Data Mutation / genetics* Oryzias / genetics* Phenotype Protein Subunits / genetics* Vacuolar Proton-Translocating ATPases / genetics* Vertebrates / genetics*
IF 3.998
引用数 1
WOS 分野 BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
メダカ Tintachina (MT977)