1i2t Citations

X-ray structure of the human hyperplastic discs protein: an ortholog of the C-terminal domain of poly(A)-binding protein.

Proc Natl Acad Sci U S A 98 4414-9 (2001)
Cited: 59 times
EuropePMC logo PMID: 11287654

Abstract

The poly(A)-binding protein (PABP) recognizes the 3' mRNA poly(A) tail and plays an essential role in eukaryotic translation initiation and mRNA stabilization/degradation. PABP is a modular protein, with four N-terminal RNA-binding domains and an extensive C terminus. The C-terminal region of PABP is essential for normal growth in yeast and has been implicated in mediating PABP homo-oligomerization and protein-protein interactions. A small, proteolytically stable, highly conserved domain has been identified within this C-terminal segment. Remarkably, this domain is also present in the hyperplastic discs protein (HYD) family of ubiquitin ligases. To better understand the function of this conserved region, an x-ray structure of the PABP-like segment of the human HYD protein has been determined at 1.04-A resolution. The conserved domain adopts a novel fold resembling a right-handed supercoil of four alpha-helices. Sequence profile searches and comparative protein structure modeling identified a small ORF from the Arabidopsis thaliana genome that encodes a structurally similar but distantly related PABP/HYD domain. Phylogenetic analysis of the experimentally determined (HYD) and homology modeled (PABP) protein surfaces revealed a conserved feature that may be responsible for binding to a PABP interacting protein, Paip1, and other shared interaction partners.

Reviews - 1i2t mentioned but not cited (1)

  1. Macromolecular ab initio phasing enforcing secondary and tertiary structure. Millán C, Sammito M, Usón I. IUCrJ 2 95-105 (2015)

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Reviews citing this publication (10)

  1. Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression. Mangus DA, Evans MC, Jacobson A. Genome Biol 4 223 (2003)
  2. Eukaryotic translation initiation factors and regulators. Sonenberg N, Dever TE. Curr Opin Struct Biol 13 56-63 (2003)
  3. Mammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects. Scheffner M, Kumar S. Biochim Biophys Acta 1843 61-74 (2014)
  4. Starting the protein synthesis machine: eukaryotic translation initiation. Preiss T, W Hentze M. Bioessays 25 1201-1211 (2003)
  5. Regulation of poly(A)-binding protein through PABP-interacting proteins. Derry MC, Yanagiya A, Martineau Y, Sonenberg N. Cold Spring Harb Symp Quant Biol 71 537-543 (2006)
  6. HECT E3s and human disease. Scheffner M, Staub O. BMC Biochem 8 Suppl 1 S6 (2007)
  7. The "tale" of poly(A) binding protein: the MLLE domain and PAM2-containing proteins. Xie J, Kozlov G, Gehring K. Biochim Biophys Acta 1839 1062-1068 (2014)
  8. Poly(A) tail synthesis and regulation: recent structural insights. Hall TM. Curr Opin Struct Biol 12 82-88 (2002)
  9. Targeting Protein Synthesis in Colorectal Cancer. Schmidt S, Denk S, Wiegering A. Cancers (Basel) 12 E1298 (2020)
  10. Weighing up the possibilities: Controlling translation by ubiquitylation and sumoylation. Watts FZ, Baldock R, Jongjitwimol J, Morley SJ. Translation (Austin) 2 e959366 (2014)

Articles citing this publication (32)