scholarly journals Structural Basis for Dynamic Interdomain Movement and RNA Recognition of the Selenocysteine-Specific Elongation Factor SelB

Structure ◽  
2007 ◽  
Vol 15 (5) ◽  
pp. 577-586 ◽  
Author(s):  
Toyoyuki Ose ◽  
Nicolas Soler ◽  
Linda Rasubala ◽  
Kimiko Kuroki ◽  
Daisuke Kohda ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Structural Basis ◽  
Rna Recognition ◽  
Specific Elongation

Structural Basis of Single-Stranded RNA Recognition

2004 ◽  
Vol 37 (5) ◽  
pp. 279-287 ◽  
Author(s):  
Ana C. Messias ◽  
Michael Sattler
Keyword(s):  
Structural Basis ◽  
Rna Recognition

scholarly journals The Selenocysteine-specific Elongation Factor Contains a Novel and Multi-functional Domain

2012 ◽  
Vol 287 (46) ◽  
pp. 38936-38945 ◽  
Author(s):  
Jonathan N. Gonzalez-Flores ◽  
Nirupama Gupta ◽  
Louise W. DeMong ◽  
Paul R. Copeland
Keyword(s):  
Elongation Factor ◽  
Functional Domain ◽  
Specific Elongation

scholarly journals Structural basis underlying CAC RNA recognition by the RRM domain of dimeric RNA-binding protein RBPMS

2015 ◽  
Vol 49 ◽  
Author(s):  
Marianna Teplova ◽  
Thalia A. Farazi ◽  
Thomas Tuschl ◽  
Dinshaw J. Patel
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Hek293 Cells ◽  
Structural Basis ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Binding Studies ◽  
Muscle Plasticity ◽  
Rrm Domain

AbstractRNA-binding protein with multiple splicing (designated RBPMS) is a higher vertebrate mRNA-binding protein containing a single RNA recognition motif (RRM). RBPMS has been shown to be involved in mRNA transport, localization and stability, with key roles in axon guidance, smooth muscle plasticity, as well as regulation of cancer cell proliferation and migration. We report on structure-function studies of the RRM domain of RBPMS bound to a CAC-containing single-stranded RNA. These results provide insights into potential topologies of complexes formed by the RBPMS RRM domain and the tandem CAC repeat binding sites as detected by photoactivatable-ribonucleoside-enhanced crosslinking and immunoprecipitation. These studies establish that the RRM domain of RBPMS forms a symmetrical dimer in the free state, with each monomer binding sequence-specifically to all three nucleotides of a CAC segment in the RNA bound state. Structure-guided mutations within the dimerization and RNA-binding interfaces of RBPMS RRM on RNA complex formation resulted in both disruption of dimerization and a decrease in RNA-binding affinity as observed by size exclusion chromatography and isothermal titration calorimetry. As anticipated from biochemical binding studies, over-expression of dimerization or RNA-binding mutants of Flag-HA-tagged RBPMS were no longer able to track with stress granules in HEK293 cells, thereby documenting the deleterious effects of such mutations in vivo.

scholarly journals Structural Basis for Nucleotide Exchange and Competition with tRNA in the Yeast Elongation Factor Complex eEF1A:eEF1Bα

2000 ◽  
Vol 6 (5) ◽  
pp. 1261-1266 ◽  
Author(s):  
Gregers Rom Andersen ◽  
Lise Pedersen ◽  
Louis Valente ◽  
Ishita Chatterjee ◽  
Terri Goss Kinzy ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Structural Basis ◽  
Nucleotide Exchange

Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (22) ◽  
pp. 6846-6857 ◽  
Author(s):  
Andrea Parmeggiani ◽  
Ivo M. Krab ◽  
Sumio Okamura ◽  
Rikke C. Nielsen ◽  
Jens Nyborg ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Structural Basis ◽  
Elongation Factor Tu

scholarly journals The Structural Basis of 5′ Triphosphate Double-Stranded RNA Recognition by RIG-I C-Terminal Domain

Structure ◽  
2010 ◽  
Vol 18 (8) ◽  
pp. 1032-1043 ◽  
Author(s):  
Cheng Lu ◽  
Hengyu Xu ◽  
C.T. Ranjith-Kumar ◽  
Monica T. Brooks ◽  
Tim Y. Hou ◽  
...  
Keyword(s):  
Structural Basis ◽  
Rna Recognition ◽  
Double Stranded Rna ◽  
Terminal Domain
Sign in / Sign up

Export Citation Format

Share Document