scholarly journals An mRNA silencing mechanism reliant on the cooperation between REGE-1/Regnase-1 and RLE-1/Roquin-1

2021 ◽  
Author(s):  
Daria Sobanska ◽  
Alicja A Komur ◽  
Agnieszka Chabowska-Kita ◽  
Julita Gumna ◽  
Pooja Kumari ◽  
...  
Keyword(s):  
Functional Relationship ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
The Other ◽  
Immune Homeostasis ◽  
C Elegans ◽  
Evolutionarily Conserved ◽  
Competing Models

Regnase-1 is an evolutionarily conserved endoribonuclease, degrading diverse mRNAs important, among others, for immune homeostasis, development, and cancer. There are two competing models of Regnase-1 mediated mRNA silencing. One model postulates that Regnase-1 works together with another RNA-binding protein, Roquin-1. The other model proposes that the two proteins function separately. Studying the C. elegans Regnase-1 ortholog, REGE-1, we have uncovered a functional relationship between REGE-1 and the nematode counterpart of Roquin-1, RLE-1. While REGE-1 and RLE-1 associate with mRNA independently of each other, both proteins are essential for mRNA silencing. Intriguingly, the functional interdependence between REGE-1 and RLE-1 is reminiscent of the proposed cooperation between mammalian Regnase-1 and Roquin-1, which may underlie a prototypic silencing mechanism involving both proteins.

scholarly journals Investigating the Roles of RNA Binding Protein Combinations in Neuronal Function and Organismal Behavior

2019 ◽  
Vol 4 (Spring 2019) ◽  
Author(s):  
Alexa Vandenburg
Keyword(s):  
Binding Sites ◽  
Neuronal Development ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Wild Type ◽  
C Elegans ◽  
Neuronal Gene ◽  
Touch Response

The Norris lab recently identified two RNA binding proteins required for proper neuron-specific splicing. The lab conducted touch- response behavioral assays to assess the function of these proteins in touch-sensing neurons. After isolating C. elegans worms with specific phenotypes, the lab used automated computer tracking and video analysis to record the worms’ behavior. The behavior of mutant worms differed from that of wild-type worms. The Norris lab also discovered two possible RNA binding protein sites in SAD-1, a neuronal gene implicated in the neuronal development of C. elegans1. These two binding sites may control the splicing of SAD-1. The lab transferred mutated DNA into the genome of wild-type worms by injecting a mutated plasmid. The newly transformed worms fluoresced green, indicating that the two binding sites control SAD-1 splicing.

FOG-2, a novel F-box containing protein, associates with the GLD-1 RNA binding protein and directs male sex determination in the C. elegans hermaphrodite germline

Development ◽  
2000 ◽  
Vol 127 (24) ◽  
pp. 5265-5276 ◽  
Author(s):  
R. Clifford ◽  
M.H. Lee ◽  
S. Nayak ◽  
M. Ohmachi ◽  
F. Giorgini ◽  
...  
Keyword(s):  
Sex Determination ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Translational Repression ◽  
Specific Substrate ◽  
Interaction Domain ◽  
C Elegans ◽  
Male Sex ◽  
F Box Protein

Male sex determination in the Caenorhabditis elegans hermaphrodite germline requires translational repression of tra-2 mRNA by the GLD-1 RNA binding protein. We cloned fog-2 by finding that its gene product physically interacts with GLD-1, forming a FOG-2/GLD-1/tra-2 3′untranslated region ternary complex. FOG-2 has an N-terminal F-box and a novel C-terminal domain called FTH. Canonical F-box proteins act as bridging components of the SCF ubiquitin ligase complex; the N-terminal F-box binds a Skp1 homolog, recruiting ubiquination machinery, while a C-terminal protein-protein interaction domain binds a specific substrate for degradation. However, since both fog-2 and gld-1 are necessary for spermatogenesis, FOG-2 cannot target GLD-1 for ubiquitin-mediated degradation. We propose that FOG-2 also acts as a bridge, bringing GLD-1 bound to tra-2 mRNA into a multiprotein translational repression complex, thus representing a novel function for an F-box protein. fog-2 is a member of a large, apparently rapidly evolving, C. elegans gene family that has expanded, in part, by local duplications; fog-2 related genes have not been found outside nematodes. fog-2 may have arisen during evolution of self-fertile hermaphroditism from an ancestral female/male species.

scholarly journals The C. elegans Polycomb Gene sop-2 Encodes an RNA Binding Protein

2004 ◽  
Vol 14 (6) ◽  
pp. 841-847 ◽  
Author(s):  
Hong Zhang ◽  
Andrea Christoforou ◽  
L Aravind ◽  
Scott W Emmons ◽  
Sander van den Heuvel ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
C Elegans

scholarly journals The double-stranded RNA binding protein RDE-4 can act cell autonomously during feeding RNAi in C. elegans

2017 ◽  
Vol 45 (14) ◽  
pp. 8463-8473 ◽  
Author(s):  
Pravrutha Raman ◽  
Soriayah M. Zaghab ◽  
Edward C. Traver ◽  
Antony M. Jose
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Double Stranded Rna ◽  
C Elegans

A conserved RNA-binding protein that regulates sexual fates in the C. elegans hermaphrodite germ line

Nature ◽  
10.1038/37297 ◽  
1997 ◽  
Vol 390 (6659) ◽  
pp. 477-484 ◽  
Author(s):  
Beilin Zhang ◽  
Maria Gallegos ◽  
Alessandro Puoti ◽  
Eileen Durkin ◽  
Stanley Fields ◽  
...  
Keyword(s):  
Rna Binding ◽  
Germ Line ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
C Elegans

scholarly journals LST-1 acts in trans with a conserved RNA-binding protein to maintain stem cells

2019 ◽  
Author(s):  
Kimberly A. Haupt ◽  
Amy L. Enright ◽  
Ahlan S. Ferdous ◽  
Aaron M. Kershner ◽  
Heaji Shin ◽  
...  
Keyword(s):  
Stem Cell ◽  
Rna Binding ◽  
Binding Protein ◽  
Regulatory Region ◽  
Rna Binding Protein ◽  
Point Mutations ◽  
Distinct Region ◽  
Protein Distribution ◽  
Self Renewal ◽  
C Elegans

ABSTRACTStem cell self-renewal is essential to development and tissue repair. The C. elegans LST-1 protein is a pivotal regulator of self-renewal and oncogenic when misexpessed. Here we define regions within the LST-1 protein that provide molecular insights into both its function and regulation. LST-1 self-renewal activity resides within a predicted disordered region that harbors two KXXL motifs. These KXXL motifs mediate LST-1 binding to FBF, a broadly conserved Pumilio/PUF RNA-binding protein that represses differentiation. Point mutations of the KXXL motifs abrogate LST-1 self-renewal activity. Therefore, FBF binding is essential to LST-1 function. A second distinct region regulates LST-1 spatial expression and primarily affects LST-1 protein turnover. Upon loss of this regulatory region, LST-1 protein distribution expands and drives formation of a larger than normal GSC pool. Thus, LST-1 promotes self-renewal as a key FBF partner, and its spatial regulation helps determine size of the GSC pool.IMPACT STATEMENTA key stem cell regulator partners with a broadly conserved PUF RNA-binding protein to drive self-renewal and maintain a stem cell pool.

Sign in / Sign up

Export Citation Format

Share Document