Protein and RNA Dynamics Play Key Roles in Determining the Specific Recognition of GU-rich Polyadenylation Regulatory Elements by Human Cstf-64 Protein

Deka, Pritilekha; Rajan, Prabhakar; Pérez‐Cañadillas, José Manuel; Varani, Gabriele

doi:10.1016/j.jmb.2005.01.046

Cited by 61 publications

(82 citation statements)

References 53 publications

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“…The interaction has a rather diffuse specificity since Cstf-64 does not recognize a specific RNA sequence or consensus but binds many GU rich RNA sequences. The dynamics profile determined by 15 N relaxation studies is also markedly different from those observed in the above examples of highly specific interaction [373]. In the free state the protein is mostly uniformly rigid in the ps-ns and µs-ms time scales.…”

Section: Protein Dynamicscontrasting

confidence: 62%

“…Detailed analysis of relaxation rates in both protein and RNA in their free and bound states, along with dynamics changes following binding have been reported for two systems, human U1A protein interaction with the 3' untranslated region (UTR) of its own pre-mRNA and VTS1p sterile alpha motif (SAM) domain interaction with the smaug recognition element (SRE) stem-loop RNA [368][369][370][371][372]. Other studies have examined dynamics in the free and RNA bound states of the cleavage stimulation factor (Cstf-64) and the ribosomal protein L11 [46,373]. Systematic characterization of RNA dynamics changes that occur on binding of a ligand has been reported for HIV-1 TAR RNA and HIV-2 TAR RNA binding to arginineamide [374,375].…”

mentioning

confidence: 99%

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Structure determination and dynamics of protein–RNA complexes by NMR spectroscopy

Dominguez

Schubert

Duss

et al. 2011

Progress in Nuclear Magnetic Resonance Spectroscopy

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Section: Protein Dynamicscontrasting

confidence: 62%

mentioning

confidence: 99%

Structure determination and dynamics of protein–RNA complexes by NMR spectroscopy

Dominguez

Schubert

Duss

et al. 2011

Progress in Nuclear Magnetic Resonance Spectroscopy

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“…Furthermore, these multiple binding sites have the ability to evolve independently. The modular architecture is also ideally suited to construct proteins that match in their RNA specificity the relatively poorly conserved sequence features observed in splicing and 3′-end processing sites of eukaryotic mRNAs [10][11][12] .…”

Section: Modularity Facilitates Functionmentioning

confidence: 99%

RNA-binding proteins: modular design for efficient function

Lunde

Moore

Varani

2007

Nat Rev Mol Cell Biol

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1,151

1,059

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Many RNA-binding proteins have modular structures, being composed of multiple repeats of just a few basic domains that are arranged in a variety of ways to satisfy their diverse functional requirements. Recent studies have investigated how different modules cooperate in regulating the RNA binding specificity and the biological activity of these proteins. They have also investigated how multiple modules cooperate with enzymatic domains to regulate the catalytic activity of enzymes acting upon RNA. These studies have shown how multiple modules define, for many RNA-binding proteins, the fundamental structural unit that is responsible for their biological function.

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“…The structure of the RRM of CstF-64 has been determined by NMR (Fig. 3B) [137], which showed the presence of a UU dinucleotide-specific binding site and that the protein:RNA interface is highly mobile [138]. This flexibility may allow CstF-64 to form stable complexes with a wide range of GU-rich sequences.…”

Section: Cstf-64 (Rna15p)mentioning

confidence: 99%

Protein factors in pre-mRNA 3′-end processing

Mandel

Bai

Tong

2007

Cell. Mol. Life Sci.

365

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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Protein and RNA Dynamics Play Key Roles in Determining the Specific Recognition of GU-rich Polyadenylation Regulatory Elements by Human Cstf-64 Protein

Cited by 61 publications

References 53 publications

Structure determination and dynamics of protein–RNA complexes by NMR spectroscopy

Structure determination and dynamics of protein–RNA complexes by NMR spectroscopy

RNA-binding proteins: modular design for efficient function

Protein factors in pre-mRNA 3′-end processing

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