PAPD1

Official Full Name

mitochondrial poly(A) polymerase

Organism

Homo sapiens

GeneID

55149

Background

The protein encoded by this gene is a member of the DNA polymerase type-B-like family. This enzyme synthesizes the 3' poly(A) tail of mitochondrial transcripts and plays a role in replication-dependent histone mRNA degradation.[provided by RefSeq, Jan 2011]

Synonyms

MTPAP; PAPD1; SPAX4; TENT6;

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Detailed Information

Structural basis for dimerization and activity of human PAPD1

In most living organisms, poly(A) polymerases (PAPs) have significant involvement in RNA function and metabolism. Also known as mtPAP, TUTase1, PAPD1 is a noncanonical PAP responsible for a mitochondrial RNAs polyadenylation, which is required to complete the stop codon (UAA) for some mitochondrial mRNAs, and RNA stability can be also probably regulated by the poly(A) tail. PAPD1 also makes great contributions to mitochondrial tRNAs maturation. The activity of PAPD1 on its own and independence from a separate RNA binding protein is contrast to GLD2. Containing a mitochondrial targeting sequence at the N terminus (residues 1-37) of PAPD1 as the sole PAP in humans is consistent with its role in the mitochondrion. Oligouridylation for uridylate histone mRNA2 by degradation of PAPD1 as well as TUTase3 suggests its functionality as a TUTase in the cytoplasm. There single-nucleotide polymorphisms (SNPs) have some relations with extreme obesity in cattle, missense mutation can be led by one of which after the mitochondrial targeting sequence.

Crystal structure of human PAPD1, which is a noncanonical PAP that can polyadenylate RNAs in mitochondria, was revealed in a recent study. Its overall structure of the palm and finger domains share some similarities with that in the canonical PAPs. Among the two domains, the active site is located with a large pocket for the accommodation of the substrates. A previously unrecognized domain in the N-terminal region of PAPD1, which is equipped with backbone fold share similarities with that of RNP-type RNA binding domains, was revealed in the structure analysis. This domain also known as the RL domain, together with β-arm insertion in the palm domain, plays a significant role in the dimerization of PAPD1, which is further confirmed to be required for the catalytic activity of PAPD1 in the mutagenesis and biochemical studies.

PAPD1 is a candidate gene for the extreme obesity related phenotype in mammals

In people with obesity, especially extreme obesity, the responsible genes remain unknown in above 95% of severe obesity cases. Amplified fragment length polyporphism (AFLP) approach was used for genome regions screening of extreme obesity-related phenotypes on divergent animals derived from Wagyu x Limousin crosses. Wagyu breed of cattle was traditionally recognized as with high intramuscular fat, while the Limousin breed is opposite to it. The two breeds with different trait have the specialty in mapping genes for obesity-related phenotypes. The newly discovered nuclear-encoded mitochondrial poly(A) polymerase, PAPD1 gene is adjacent at the human gene KIAA1462 on the chromosome, and has an enrollment in RNA processing for the requirement of polyadenylation and stabilization of mammalian mitochondrial mRNAs.

Figure 1. Comparative annotation of both cDNA and genomic DNA sequences of the bovine PAPD1 gene. (Xiao, et al. 2006)

References:

Xiao Q, Wu X L, Michal J J, et al. A novel nuclear-encoded mitochondrial poly (A) polymerase PAPD1 is a potential candidate gene for the extreme obesity related phenotypes in mammals. International journal of biological sciences, 2006, 2(4): 171.
Bai Y, Srivastava S K, Chang J H, et al. Structural basis for dimerization and activity of human PAPD1, a noncanonical poly (A) polymerase. Molecular cell, 2011, 41(3): 311-320.

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