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Crystal structure of human poly(A) polymerase gamma reveals a conserved catalytic core for canonical poly(A) polymerases

Yang, Q. and Nausch, L. W. and Martin, G. and Keller, W. and Doublié, S.. (2013) Crystal structure of human poly(A) polymerase gamma reveals a conserved catalytic core for canonical poly(A) polymerases. Journal of Molecular Biology, 426 (1). pp. 43-50.

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Official URL: http://edoc.unibas.ch/dok/A6211855

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Abstract

In eukaryotes, the poly(A) tail added at the 3′ end of an mRNA precursor is essential for the regulation ofmRNA stability and the initiation of translation. Poly(A) polymerase (PAP) is the enzyme that catalyzes thepoly(A) addition reaction. Multiple isoforms of PAP have been identified in vertebrates, which originate fromgene duplication, alternative splicing or post-translational modifications. The complexity of PAP isoformssuggests that they might play different roles in the cell. Phylogenetic studies indicate that vertebrate PAPs aregrouped into three clades termed α, β and γ, which originated from two gene duplication events. To date, allthe available PAP structures are from the PAPα clade. Here, we present the crystal structure of the firstrepresentative of the PAPγ clade, human PAPγ bound to cordycepin triphosphate (3′dATP) and Ca2+. Thestructure revealed that PAPγ closely resembles its PAPα ortholog. An analysis of residue conservationreveals a conserved catalytic binding pocket, whereas residues at the surface of the polymerase are moredivergent.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Cell Biology (Keller)
05 Faculty of Science > Departement Biozentrum > Growth & Development
UniBasel Contributors:Martin, Georges and Keller, Walter
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Elsevier
ISSN:0022-2836
e-ISSN:1089-8638
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:08 Nov 2017 08:29
Deposited On:31 Jan 2014 09:50

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