Exploring the role of elongation Factor-Like 1 (EFL1) in Shwachman-Diamond syndrome through molecular dynamics


Por: Delre, Pietro, Alberga, Domenico, Gijsbers, Abril, Sanchez-Puig, Nuria, Nicolotti, Orazio, Saviano, Michele, Siliqi, Dritan, Mangiatordi, Giuseppe Felice

Publicada: 21 nov 2020 Ahead of Print: 1 dic 2019
Resumen:
Shwachman-Diamond Syndrome (SDS) is an autosomal recessive disorder whose patients present mutations in two ribosome assembly proteins, the Shwachman-Bodian-Diamond Syndrome protein (SBDS) and the Elongation Factor-Like 1 (EFL1). Due to the lack of knowledge of the molecular mechanisms responsible for SDS pathogenesis, current therapy is nonspecific and focuses only at alleviating the symptoms. Building on the recent observation that EFL1 single-point mutations clinically manifest as SDS-like phenotype, we carried out comparative Molecular Dynamics (MD) simulations on three mutants, T127A, M882K and R1095Q and wild type EFL1. As supported by small angle X-ray scattering experiments, the obtained data improve the static EFL1 model resulting from the Cryo-electron microscopy and clearly show that all the mutants experience a peculiar rotation, around the hinge region, of domain IV with respect to domains I and II leading to a different conformation respect to that of wild type protein. This study supports the notion that EFL1 function is governed by an allosteric mechanism involving the concerted action of GTPase domain (domain I) and the domain IV and can help point towards new approaches to SDS treatment. Communicated by Ramaswamy H. Sarma

Filiaciones:
Delre, Pietro:
 Dipartimento di Chimica, Università Degli Studi di Bari “Aldo Moro”, Bari, Italy

 Consiglio Nazionale Delle Ricerche, Istituto di Cristallografia, Bari, Italy

Alberga, Domenico:
 Cineca, Casalecchio di Reno, Italy

Gijsbers, Abril:
 The Maastricht Multimodal Molecular Imaging Institute (M4I), Division of Nanoscopy, Maastricht University, Maastricht, Netherlands

Sanchez-Puig, Nuria:
 Instituto de Química, Universidad Nacional Autónoma de México, Ciudad Universitaria, Ciudad de México, Mexico

Nicolotti, Orazio:
 Dipartimento di Farmacia—Scienze Del Farmaco, Università` Degli Studi di Bari “Aldo Moro”, Bari, Italy

Saviano, Michele:
 Consiglio Nazionale Delle Ricerche, Istituto di Cristallografia, Bari, Italy

Siliqi, Dritan:
 Consiglio Nazionale Delle Ricerche, Istituto di Cristallografia, Bari, Italy

Mangiatordi, Giuseppe Felice:
 Consiglio Nazionale Delle Ricerche, Istituto di Cristallografia, Bari, Italy
ISSN: 07391102





JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Editorial
ADENINE PRESS, 2066 CENTRAL AVE, SCHENECTADY, NY 12304 USA, Estados Unidos America
Tipo de documento: Article
Volumen: 38 Número: 17
Páginas: 5219-5229
WOS Id: 000503709600001
ID de PubMed: 31838967