Abstract. PPARGC1A exerts important functions in activating many nuclear receptors and
transcription factors that are related to energy balance. Previous studies have
shown that PPARGC1A gene is associated with lactation traits of dairy cattle.
However, the functional role of the buffalo PPARGC1A gene is still unknown. In this
work, the complete coding sequence (CDS) of buffalo PPARGC1A was isolated and
characterized for swamp and river buffalo. The CDS length of PPARGC1A for both types
of buffalo was the same, which was composed of 2394 nucleotides and encoded
a peptide composed of 797 amino acid residues. This protein belonged to a
hydrophilic protein and contained one RRM_PPARGC1A domain (AA 674–764) without a signal peptide or a transmembrane domain. The
differential expressions of this gene in 10 buffalo tissues in lactation and
non-lactation displayed that the PPARGC1A was highly expressed in the muscle, heart,
liver, brain and kidney of both non-lactating and lactating periods, but its
expression was significantly different in the muscle, heart, liver, small
intestine, mammary gland, rumen, spleen and lung between the two periods.
Eight single nucleotide polymorphisms (SNPs) were found in buffalo, in which
the c.778C>T, c.1257G>A and c.1311G>A
were shared by two types of buffalo with similar allele frequencies, while
the c.419C>T, c.759A>G, c.920C>A,
c.926G>A and c.1509A>T were only observed in river
buffalo. The SNP419, SNP920 and SNP926 were non-synonymous, which led to the
amino acid changes of p.Ser140Phe, p.Pro307His and p.Arg309Lys. Seven
nucleotide differential sites were identified in the PPARGC1A gene between buffalo and
other Bovidae species. Phylogenetic analysis indicated that buffaloes were
independently clustered into one branch, but they were closely related to
the species of the Bos genus. The results indicate that buffalo PPARGC1A is an
inducible transcriptional coactivator involved in regulating carbohydrate
and fat metabolism. It can exert a functional role in a variety of buffalo
tissues and may participate in milk fat synthesis and development in the
mammary gland.
Functional role of polar amino acid residues in Na+/H+ exchangers
