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RNA recognition and self-association of CPEB4 is mediated by its tandem RRM domains.

Schelhorn C, Gordon JM, Ruiz L, Alguacil J, Pedroso E, Macias MJ - Nucleic Acids Res. (2014)

Bottom Line: Self-association does not affect the proteins' ability to interact with RNA as demonstrated by ion mobility-mass spectrometry.Chemical shift effects measured by NMR of the apo forms of the RRM1-RRM2 samples indicate that the two domains are orientated toward each other.We propose a model of the CPEB4 RRM1-RRM2-CPE complex that illustrates the experimental data.

View Article: PubMed Central - PubMed

Affiliation: Institute for Research in Biomedicine (IRB Barcelona), Baldiri Reixac 10, Barcelona 08028, Spain.

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Alignment was prepared using the Geneious R6 software (biomatters). The position of the RRM domains is indicated and the RNP motifs highlighted. Black residues are conserved between all family members. Gray residues are partially conserved and blank residues are un-conserved.
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Figure 1: Alignment was prepared using the Geneious R6 software (biomatters). The position of the RRM domains is indicated and the RNP motifs highlighted. Black residues are conserved between all family members. Gray residues are partially conserved and blank residues are un-conserved.

Mentions: The structure of the RRM1 domain of CPEB3, which is completely conserved when aligned to CPEB2 and 4, has been solved byNuclear Magnetic Resonance (NMR) (PDB code: 2DNL) and shows the canonical RRM domain fold of a αβ-sandwich with a β1α1β2β3α2β4 topology with the addition of two β strands immediately before the β4 strand (β4′ and β4″). Two conserved motifs, which are generally involved in RRM–RNA interactions, RNP1 and RNP2 lie in the central strands of the RRM β-sheet (18). The consensus sequence of RNP1 is (RK)-G-(FY)-(GA)-(FY)-(ILV)-X-(FY), while that of RNP2 is (ILV)-(FY)-(ILV)-X-N-L. The first RRM domain (RRM1) contains, for the most part, both RNP motifs. However, the second (RRM2), more C-terminal domain lacks the consensus sequence of an RNP1 motif. This characteristic is shared among all CPEB family members (Figure 1).


RNA recognition and self-association of CPEB4 is mediated by its tandem RRM domains.

Schelhorn C, Gordon JM, Ruiz L, Alguacil J, Pedroso E, Macias MJ - Nucleic Acids Res. (2014)

Alignment was prepared using the Geneious R6 software (biomatters). The position of the RRM domains is indicated and the RNP motifs highlighted. Black residues are conserved between all family members. Gray residues are partially conserved and blank residues are un-conserved.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4150798&req=5

Figure 1: Alignment was prepared using the Geneious R6 software (biomatters). The position of the RRM domains is indicated and the RNP motifs highlighted. Black residues are conserved between all family members. Gray residues are partially conserved and blank residues are un-conserved.
Mentions: The structure of the RRM1 domain of CPEB3, which is completely conserved when aligned to CPEB2 and 4, has been solved byNuclear Magnetic Resonance (NMR) (PDB code: 2DNL) and shows the canonical RRM domain fold of a αβ-sandwich with a β1α1β2β3α2β4 topology with the addition of two β strands immediately before the β4 strand (β4′ and β4″). Two conserved motifs, which are generally involved in RRM–RNA interactions, RNP1 and RNP2 lie in the central strands of the RRM β-sheet (18). The consensus sequence of RNP1 is (RK)-G-(FY)-(GA)-(FY)-(ILV)-X-(FY), while that of RNP2 is (ILV)-(FY)-(ILV)-X-N-L. The first RRM domain (RRM1) contains, for the most part, both RNP motifs. However, the second (RRM2), more C-terminal domain lacks the consensus sequence of an RNP1 motif. This characteristic is shared among all CPEB family members (Figure 1).

Bottom Line: Self-association does not affect the proteins' ability to interact with RNA as demonstrated by ion mobility-mass spectrometry.Chemical shift effects measured by NMR of the apo forms of the RRM1-RRM2 samples indicate that the two domains are orientated toward each other.We propose a model of the CPEB4 RRM1-RRM2-CPE complex that illustrates the experimental data.

View Article: PubMed Central - PubMed

Affiliation: Institute for Research in Biomedicine (IRB Barcelona), Baldiri Reixac 10, Barcelona 08028, Spain.

Show MeSH
Related in: MedlinePlus