Solution Structure of the Second RNA Recognition Motif (RRM) Domain of Murine T Cell Intracellular Antigen-1 (TIA-1) and Its RNA Recognition Mode†‡

Biochemistry ◽  
2008 ◽  
Vol 47 (24) ◽  
pp. 6437-6450 ◽  
Author(s):  
Kanako Kuwasako ◽  
Mari Takahashi ◽  
Naoya Tochio ◽  
Chikage Abe ◽  
Kengo Tsuda ◽  
...  
Keyword(s):  
T Cell ◽  
Solution Structure ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif ◽  
Rrm Domain ◽  
Intracellular Antigen

scholarly journals RNA Binding of T-cell Intracellular Antigen-1 (TIA-1) C-terminal RNA Recognition Motif Is Modified by pH Conditions

2013 ◽  
Vol 288 (36) ◽  
pp. 25986-25994 ◽  
Author(s):  
Isabel Cruz-Gallardo ◽  
Ángeles Aroca ◽  
Cecilia Persson ◽  
B. Göran Karlsson ◽  
Irene Díaz-Moreno
Keyword(s):  
T Cell ◽  
Rna Binding ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif ◽  
Intracellular Antigen ◽  
Ph Conditions

scholarly journals Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment

2016 ◽  
Vol 26 (2) ◽  
pp. 280-291 ◽  
Author(s):  
Kanako Kuwasako ◽  
Nobukazu Nameki ◽  
Kengo Tsuda ◽  
Mari Takahashi ◽  
Atsuko Sato ◽  
...  
Keyword(s):  
Solution Structure ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif ◽  
Spliceosomal Protein

scholarly journals Structural studies on the RNA-recognition motif of NELF E, a cellular negative transcription elongation factor involved in the regulation of HIV transcription

2006 ◽  
Vol 400 (3) ◽  
pp. 449-456 ◽  
Author(s):  
Jampani N. Rao ◽  
Liane Neumann ◽  
Sabine Wenzel ◽  
Kristian Schweimer ◽  
Paul Rösch ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Solution Structure ◽  
Rna Binding ◽  
Transcription Elongation ◽  
Elongation Factor ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif ◽  
Transcription Elongation Factor ◽  
Tar Rna

The elongation of transcription of HIV RNA at the TAR (transactivation-response element) is highly regulated by positive and negative factors. The cellular negative transcription elongation factor NELF (negative elongation factor) was suggested to be involved in transcriptional regulation of HIV-1 (HIV type 1) by binding to the stem of the viral TAR RNA which is synthesized by cellular RNA polymerase II at the viral long terminal repeat. NELF is a heterotetrameric protein consisting of NELF A, B, C or the splice variant D, and E. In the present study, we determined the solution structure of the RRM (RNA-recognition motif) of the RNA-binding subunit NELF E and studied its interaction with the viral TAR RNA. Our results show that the separately expressed recombinant NELF E RRM has α-helical and β-strand elements adopting a βαββαβ fold and is able to bind to TAR RNA. Fluorescence equilibrium titrations with fluorescently labelled double- and single-stranded oligoribonucleotides representing the TAR RNA stem imply that NELF E RRM binds to the single-stranded TAR RNAs with Kd values in the low-micromolar range.

A conserved RNA recognition motif (RRM) domain of Brassica napus FCA improves cotton fiber quality and yield by regulating cell size

2011 ◽  
Vol 30 (1) ◽  
pp. 93-101 ◽  
Author(s):  
Fan Sun ◽  
Chuanliang Liu ◽  
Chaojun Zhang ◽  
Weiwei Qi ◽  
Xueyan Zhang ◽  
...  
Keyword(s):  
Brassica Napus ◽  
Cell Size ◽  
Cotton Fiber ◽  
Fiber Quality ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif ◽  
Rrm Domain ◽  
Cotton Fiber Quality

scholarly journals RRM domain of ALS/FTD-causing FUS interacts with membrane: an anchor of membraneless organelles to membranes?

2017 ◽  
Author(s):  
Yimei Lu ◽  
Liangzhong Lim ◽  
Jianxing Song
Keyword(s):  
Significant Interaction ◽  
Bilayer Membrane ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Large Network ◽  
Sequence Complexity ◽  
Recognition Motif ◽  
Rrm Domain ◽  
In Cells

Abstract526-residue FUS functions to self-assemble into reversible droplets/hydrogels, which could be further solidified into pathological fibrils. FUS is composed of N-terminal low-sequence complexity (LC); RNA-recognition motif (RRM) and C-terminal LC domains. FUS belongs to an emerging category of proteins which are capable of forming membraneless organelles in cells via phase separation. On the other hand, eukaryotic cells contain a large network of internal membrane systems. Therefore, it is of fundamental importance to address whether membraneless organelles can interact with membranes. Here we attempted to explore this by NMR HSQC titrations of three FUS domains with gradual addition of DMPC/DHPC bicelle, which mimics the bilayer membrane. We found that both N- and C-terminal LC domains showed no significant interaction with bicelle, but its well-folded RRM domain does dynamically interact with bicelle with an interface opposite to that for binding nucleic acids including RNA and ssDNA. If this in vitro observation also occurs in cells, to interact with membrane might represent a mechanism for dynamically organizing membraneless organelles to membranes to facilitate their physiological functions.

scholarly journals Crystal structure of human Acinus RNA recognition motif domain

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e5163 ◽  
Author(s):  
Humberto Fernandes ◽  
Honorata Czapinska ◽  
Katarzyna Grudziaz ◽  
Janusz M. Bujnicki ◽  
Martyna Nowacka
Keyword(s):  
Crystal Structure ◽  
Rna Binding ◽  
Chromatin Condensation ◽  
Rna Recognition Motif ◽  
Target Sequence ◽  
Rna Recognition ◽  
Recognition Motif ◽  
Rrm Domain ◽  
Α Helix ◽  
Β Sheet

Acinus is an abundant nuclear protein involved in apoptosis and splicing. It has been implicated in inducing apoptotic chromatin condensation and DNA fragmentation during programmed cell death. Acinus undergoes activation by proteolytic cleavage that produces a truncated p17 form that comprises only the RNA recognition motif (RRM) domain. We have determined the crystal structure of the human Acinus RRM domain (AcRRM) at 1.65 Å resolution. It shows a classical four-stranded antiparallel β-sheet fold with two flanking α-helices and an additional, non-classical α-helix at the C-terminus, which harbors the caspase-3 target sequence that is cleaved during Acinus activation. In the structure, the C-terminal α-helix partially occludes the potential ligand binding surface of the β-sheet and hypothetically shields it from non-sequence specific interactions with RNA. Based on the comparison with other RRM-RNA complex structures, it is likely that the C-terminal α-helix changes its conformation with respect to the RRM core in order to enable RNA binding by Acinus.

Sign in / Sign up

Export Citation Format

Share Document