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Biomol NMR Assign. 2019 Jan 10. doi: 10.1007/s12104-019-09871-4. [Epub ahead of print]

Resonance assignment of human LARP4A La module.

Author information

1
Randall Centre for Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.
2
Department of Chemistry, King's College London, 7 Trinity Street, London, SE1 1DB, UK.
3
The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
4
Department of Pharmacy, University of Naples Federico II, Naples, Italy.
5
Institute of Protein Biochemistry, National Research Council, Via Pietro Castellino 111, 80131, Naples, Italy.
6
MRC Biomedical NMR Centre, The Francis Crick Institute, London, NW1 1AT, UK.
7
Centre for Biomolecular Spectroscopy, King's College London, London, SE1 1UL, UK.
8
Randall Centre for Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK. sasi.conte@kcl.ac.uk.
9
Centre for Biomolecular Spectroscopy, King's College London, London, SE1 1UL, UK. sasi.conte@kcl.ac.uk.

Abstract

Human LARP4A belongs to a superfamily of RNA binding proteins called La-related proteins (LARPs). Whilst being a positive regulator of protein synthesis and a promoter of mRNA stability, LARP4A also controls cell morphology and motility in human breast and prostate cancer cells. All LARPs share a characteristic RNA binding unit named the La-module, which despite a high level of primary structure conservation exhibits a great versatility in RNA target selection. Human LARP4A La-module is the most divergent compared with other LARPs and its RNA recognition properties have only recently started to be revealed. Given the key role of LARP4A protein in cancer cell biology, we have initiated a complete NMR characterisation of its La-module and here we report the assignment of 1H, 15N and 13C resonances resulting from our studies.

KEYWORDS:

LARP4A; LARPs; La–module; RNA binding protein

PMID:
30632004
DOI:
10.1007/s12104-019-09871-4

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