The nuclear poly(A) binding protein, PABP2, forms an oligomeric particle covering the length of the poly(A) tail

Keller, Rebecca W.; Kühn, U.; Aragón, Mateo; Bornikova, Larissa; Wahle, Elmar; Bear, David G.

doi:10.1006/jmbi.2000.3572

Cited by 67 publications

(77 citation statements)

References 56 publications

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“…This is compatible with an earlier observation that the CTD (arginine rich) can also self-associate (193). In fact, in the absence of poly(A) and at elevated concentrations, PABPN1 is prone to aggregation into oligomers (194,195). Each PABPN1 can recognize an ϳ10-nt poly(A) sequence (195).…”

Section: Pabpn1supporting

confidence: 91%

Delineating the Structural Blueprint of the Pre-mRNA 3′-End Processing Machinery

Xiang

Tong

Manley

2014

Molecular and Cellular Biology

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Processing of mRNA precursors (pre-mRNAs) by polyadenylation is an essential step in gene expression. Polyadenylation consists of two steps, cleavage and poly(A) synthesis, and requires multiple cis elements in the pre-mRNA and a megadalton protein complex bearing the two essential enzymatic activities. While genetic and biochemical studies remain the major approaches in characterizing these factors, structural biology has emerged during the past decade to help understand the molecular assembly and mechanistic details of the process. With structural information about more proteins and higher-order complexes becoming available, we are coming closer to obtaining a structural blueprint of the polyadenylation machinery that explains both how this complex functions and how it is regulated and connected to other cellular processes.

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Section: Pabpn1supporting

confidence: 91%

Delineating the Structural Blueprint of the Pre-mRNA 3′-End Processing Machinery

Xiang

Tong

Manley

2014

Molecular and Cellular Biology

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“…The relatively homogeneous length of the poly(A) tails synthesized in this reconstituted in vitro reaction corresponds to the length of newly synthesized poly(A) tails in vivo . PABPN1 is essential for this length control (Wahle , 1995 ;Keller et al , 2000 ;. This model is supported by several in vivo observations, including a modest decrease in steady-state poly(A) tail length upon knockdown of PABPN1 in primary mouse myoblasts (Chen et al , 1999b ;Benoit et al , 2005 ;Apponi et al , 2010 ).…”

Section: The Nuclear Poly(a)-binding Proteinsupporting

confidence: 59%

“…As described above, the functional unit of PABPN1 in RNA binding is a monomer. Nevertheless, functionally relevant oligomerization is indicated by a modest degree of cooperativity in RNA binding (Meyer et al , 2002 ;, and the formation of a higher order structure of the poly(A)-PABPN1 complex may be important for polyadenylation and length control (Keller et al , 2000 ;. Although the RRM of PABPN1 can dimerize (see above), the C-terminal domain also contributes to homotypic interactions and is responsible for the cooperativity of RNA binding (Fan et al , 2001 ;.…”

Section: Functional Consequences Of Pabpn1 Methylationmentioning

confidence: 99%

Methylation of the nuclear poly(A)-binding protein by type I protein arginine methyltransferases – how and why

Wahle

Moritz²

2013

Biological Chemistry

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Asymmetric dimethylation of arginine side chains in proteins is a frequent posttranslational modification, catalyzed by type I protein arginine methyltransferases (PRMTs). This article summarizes what is known about this modification in the nuclear poly(A)-binding protein (PABPN1). PABPN1 contains 13 dimethylated arginine residues in its C-terminal domain. Three enzymes, PRMT1, 3, and 6, can methylate PABPN1. Although 26 methyl groups are transferred to one PABPN1 molecule, the PRMTs do so in a distributive reaction, i.e., only a single methyl group is transferred per binding event. As PRMTs form dimers, with the active sites accessible from a small central cavity, backbone conformation around the methyl-accepting arginine is an important determinant of substrate specificity. Neither the association of PABPN1 with poly(A) nor its role in poly(A) tail synthesis is affected by arginine methylation. At least at low protein concentration, methylation does not affect the protein ' s tendency to oligomerize. The dimethylarginine residues of PABPN1 are located in the binding site for its nuclear import receptor, transportin. Arginine methylation weakens this interaction about 10-fold. Very recent evidence suggests that arginine methylation as a way of fine-tuning the interactions between transportin and its cargo may be a general mechanism.

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“…The polyadenylation reaction can occur without PABP, but controlling the length of the poly(A) tail requires PABP [192][193][194][195]. PABP binds directly to nascent stretches of 11-14 adenylate nucleotides as they become available [196], and this binding continues until the proper poly(A) tail length is reached (~200 to 300 bases in mammals) [197]. In addition, direct binding of PABP to premRNA, adjacent to PAP, increases the efficiency of polyadenylation 80-fold [198].…”

Section: Poly(a) Binding Proteinmentioning

confidence: 99%

Protein factors in pre-mRNA 3′-end processing

Mandel

Bai

Tong

2007

Cell. Mol. Life Sci.

357

482

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Most eukaryotic mRNA precursors (pre-mRNAs) must undergo extensive processing, including cleavage and polyadenylation at the 3′-end. Processing at the 3′-end is controlled by sequence elements in the pre-mRNA (cis elements) as well as protein factors. Despite the seeming biochemical simplicity of the processing reactions, more than 14 proteins have been identified for the mammalian complex, and more than 20 proteins have been identified for the yeast complex. The 3′-end processing machinery also has important roles in transcription and splicing. The mammalian machinery contains several sub-complexes, including cleavage and polyadenylation specificity factor (CPSF), cleavage stimulation factor (CstF), cleavage factor I (CF I m ), and cleavage factor II (CF II m ). Additional protein factors include poly(A) polymerase (PAP), poly(A) binding protein (PABP), symplekin, and the C-terminal domain (CTD) of RNA polymerase II largest subunit. The yeast machinery includes cleavage factor IA (CF IA), cleavage factor IB (CF IB), and cleavage and polyadenylation factor (CPF).

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The nuclear poly(A) binding protein, PABP2, forms an oligomeric particle covering the length of the poly(A) tail

Cited by 67 publications

References 56 publications

Delineating the Structural Blueprint of the Pre-mRNA 3′-End Processing Machinery

Delineating the Structural Blueprint of the Pre-mRNA 3′-End Processing Machinery

Methylation of the nuclear poly(A)-binding protein by type I protein arginine methyltransferases – how and why

Protein factors in pre-mRNA 3′-end processing

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