Resonance assignment of human LARP4A La module

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

doi:10.1007/s12104-019-09871-4

Resonance assignment of human LARP4A La module

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

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

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 ¹ H, ¹⁵ N and ¹³ C resonances resulting from our studies.

Original language	English
Pages (from-to)	169-172
Number of pages	4
Journal	Biomolecular NMR Assignments
Volume	13
Issue number	1
DOIs	https://doi.org/10.1007/s12104-019-09871-4
State	Published - 1 Apr 2019
Externally published	Yes

Keywords

LARP4A
LARPs
La–module
RNA binding protein

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10.1007/s12104-019-09871-4

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title = "Resonance assignment of human LARP4A La module",

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 1 H, 15 N and 13 C resonances resulting from our studies.",

keywords = "LARP4A, LARPs, La–module, RNA binding protein",

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AU - Cruz-Gallardo, Isabel

AU - Martino, Luigi

AU - Trotta, Roberta

AU - De Tito, Stefano

AU - Kelly, Geoff

AU - Atkinson, R. Andrew

AU - Randazzo, Antonio

AU - Conte, Maria R.

PY - 2019/4/1

Y1 - 2019/4/1

N2 - 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 1 H, 15 N and 13 C resonances resulting from our studies.

AB - 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 1 H, 15 N and 13 C resonances resulting from our studies.

KW - LARP4A

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Resonance assignment of human LARP4A La module

Abstract

Keywords

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