Resonance assignment of human LARP4A La module
journal contributionposted on 12.12.2019 by Isabel Cruz-Gallardo, Luigi Martino, Roberta Trotta, Stefano De Tito, Geoff Kelly, R Andrew Atkinson, Antonio Randazzo, Maria R Conte
Any type of content formally published in an academic journal, usually following a peer-review process.
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.