Resonance assignment of human LARP4A La module

Isabel Cruz-Gallardo,Stefano De Tito,Geoff Kelly,Luigi Martino,R Andrew Atkinson,Maria R Conte,Antonio Randazzo,Roberta Trotta

doi:10.1007/s12104-019-09871-4

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.

Highlights

Human LARP4A is an RNA binding protein (RBP) involved in mRNA stabilisation and translation enhancement, 3′UTR polyA lengthening and miRNA processing (Maraia et al 2017; Mattijssen et al 2017; Nussbacher and Yeo 2018; Yang et al 2011)
How the cellular functions of LARP4A in RNA and tumour biology are mediated by its molecular associations to RNA targets and/or other proteins remains unclear
LARP4A possesses a La–module, a unique RNA binding unit conserved across all the members of the La-related proteins (LARPs) superfamily and consisting of two domains, the La motif (LaM) and an RNA recognition motif (RRM1) (Bousquet-Antonelli and Deragon 2009; Maraia et al 2017)

Summary

Introduction

Human LARP4A is an RNA binding protein (RBP) involved in mRNA stabilisation and translation enhancement, 3′UTR polyA lengthening and miRNA processing (Maraia et al 2017; Mattijssen et al 2017; Nussbacher and Yeo 2018; Yang et al 2011). Keywords LARP4A · La–module · LARPs · RNA binding protein 3 MRC Biomedical NMR Centre, The Francis Crick Institute, London NW1 1AT, UK

Results

Conclusion