Cooperative energetic effects elicited by the yeast Shwachman-Diamond syndrome protein (Sdo1) and guanine nucleotides modulate the complex conformational landscape of the elongation factor-like 1 (Efl1) GTPase

2019 ◽  
Vol 247 ◽  
pp. 13-24 ◽  
Author(s):  
Axel Luviano ◽  
Roberto Cruz-Castañeda ◽  
Nuria Sánchez-Puig ◽  
Enrique García-Hernández
Keyword(s):  
Elongation Factor ◽  
Guanine Nucleotides ◽  
Conformational Landscape ◽  
Shwachman Diamond Syndrome ◽  
Syndrome Protein

scholarly journals Interaction of the GTPase Elongation Factor Like-1 with the Shwachman-Diamond Syndrome Protein and Its Missense Mutations

2018 ◽  
Vol 19 (12) ◽  
pp. 4012 ◽  
Author(s):  
Abril Gijsbers ◽  
Diana Montagut ◽  
Alfonso Méndez-Godoy ◽  
Davide Altamura ◽  
Michele Saviano ◽  
...  
Keyword(s):  
Ribosomal Subunit ◽  
Interaction Mechanism ◽  
Elongation Factor ◽  
Missense Mutations ◽  
Molecular Alterations ◽  
X Ray Scattering ◽  
Genes Encoding ◽  
Initial Interaction ◽  
Shwachman Diamond Syndrome ◽  
Syndrome Protein

The Shwachman-Diamond Syndrome (SDS) is a disorder arising from mutations in the genes encoding for the Shwachman-Bodian-Diamond Syndrome (SBDS) protein and the GTPase known as Elongation Factor Like-1 (EFL1). Together, these proteins remove the anti-association factor eIF6 from the surface of the pre-60S ribosomal subunit to promote the formation of mature ribosomes. SBDS missense mutations can either destabilize the protein fold or affect surface epitopes. The molecular alterations resulting from the latter remain largely unknown, although some evidence suggest that binding to EFL1 may be affected. We further explored the effect of these SBDS mutations on the interaction with EFL1, and showed that all tested mutations disrupted the binding to EFL1. Binding was either severely weakened or almost abolished, depending on the assessed mutation. In higher eukaryotes, SBDS is essential for development, and lack of the protein results in early lethality. The existence of patients whose only source of SBDS consists of that with surface missense mutations highlights the importance of the interaction with EFL1 for their function. Additionally, we studied the interaction mechanism of the proteins in solution and demonstrated that binding consists of two independent and cooperative events, with domains 2–3 of SBDS directing the initial interaction with EFL1, followed by docking of domain 1. In solution, both proteins exhibited large flexibility and consisted of an ensemble of conformations, as demonstrated by Small Angle X-ray Scattering (SAXS) experiments.

An isotope edited classical Raman difference spectroscopic study of the interactions of guanine nucleotides with elongation factor Tu and H-ras p21

Biochemistry ◽  
1991 ◽  
Vol 30 (45) ◽  
pp. 10914-10920 ◽  
Author(s):  
Danny Manor ◽  
Gezhi Weng ◽  
Hua Deng ◽  
Sharon Cosloy ◽  
Cun Xiang Chen ◽  
...  
Keyword(s):  
Spectroscopic Study ◽  
Elongation Factor ◽  
Guanine Nucleotides ◽  
Elongation Factor Tu ◽  
Ras P21

scholarly journals Shwachman-Diamond Syndrome Protein SBDS Maintains Human Telomeres by Regulating Telomerase Recruitment

Cell Reports ◽  
2018 ◽  
Vol 22 (7) ◽  
pp. 1849-1860 ◽  
Author(s):  
Yi Liu ◽  
Feng Liu ◽  
Yizhao Cao ◽  
Huimin Xu ◽  
Yangxiu Wu ◽  
...  
Keyword(s):  
Shwachman Diamond Syndrome ◽  
Syndrome Protein
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