scholarly journals A mRNA localized to the vegetal cortex of Xenopus oocytes encodes a protein with a nanos-like zinc finger domain

Development ◽  
1993 ◽  
Vol 117 (1) ◽  
pp. 377-386 ◽  
Author(s):  
L. Mosquera ◽  
C. Forristall ◽  
Y. Zhou ◽  
M.L. King
Keyword(s):  
Cell Fate ◽  
Zinc Finger ◽  
Regional Differences ◽  
Xenopus Oocytes ◽  
Rna Binding ◽  
Protein Product ◽  
Posterior Pole ◽  
Cortical Region ◽  
Zinc Finger Domain ◽  
Vegetal Cortex

mRNAs concentrated in specific regions of the oocyte have been found to encode determinants that specify cell fate. We show that an intermediate filament fraction isolated from Xenopus stage VI oocytes specifically contains, in addition to Vg1 RNA, a new localized mRNA, Xcat-2. Like Vg1, Xcat-2 is found in the vegetal cortical region, is inherited by the vegetal blasomeres during development, and is degraded very early in development. Sequence analysis suggests that Xcat-2 encodes a protein that belongs to the CCHC RNA-binding family of zinc finger proteins. Interestingly, the closest known relative to Xcat-2 in this family is nanos, an RNA localized to the posterior pole of the Drosophila oocyte whose protein product suppresses the translation of the transcription factor hunchback. The localized and maternally restricted expression of Xcat-2 RNA suggests a role for its protein in setting up regional differences in gene expression that occur early in development.

fatvg encodes a new localized RNA that uses a 25-nucleotide element (FVLE1) to localize to the vegetal cortex of Xenopus oocytes

Development ◽  
1999 ◽  
Vol 126 (22) ◽  
pp. 4943-4953 ◽  
Author(s):  
A.P. Chan ◽  
M. Kloc ◽  
L.D. Etkin
Keyword(s):  
Cell Fate ◽  
Xenopus Oocytes ◽  
Single Copy ◽  
Biological Functions ◽  
Embryonic Patterning ◽  
Cis Acting ◽  
Maternal Transcript ◽  
Vegetal Cortex ◽  
Mitochondrial Cloud ◽  
Localization Elements

Vegetally localized transcripts have been implicated in a number of important biological functions, including cell fate determination and embryonic patterning. We have isolated a cDNA, fatvg, which encodes a localized maternal transcript that exhibits a localization pattern reminiscent of Vg1 mRNA. fatvg is the homologue of a mammalian gene expressed in adipose tissues. The fatvg transcript, unlike Vg1 which localizes strictly through the Late pathway, also associates with the mitochondrial cloud that is characteristic of the METRO or Early pathway. This suggests that fatvg mRNA may utilize both the METRO and Late pathways to localize to the vegetal cortex during oogenesis. We have dissected the cis-acting localization elements of fatvg mRNA and compared these elements with Vg1 mRNA. Our results indicate that, like most localized RNAs, in a variety of systems, transcripts of fatvg contain localization elements in the 3′UTR. The 3′UTR of fatvg mRNA contains multiple elements that are able to function independently; however, it functions most efficiently when all of the elements are present. We have defined a short 25-nucleotide element that can direct vegetal localization as a single copy. This element differs in sequence from previously described Vg1 localization elements, suggesting that different localization elements are involved in the localization of RNAs through the Late pathway.

scholarly journals The APC/CFZY–1/Cdc20 Complex Coordinates With OMA-1 to Regulate the Oocyte-to-Embryo Transition in Caenorhabditis elegans

2021 ◽  
Vol 9 ◽  
Author(s):  
Yabing Hu ◽  
Xuewen Hu ◽  
Dongchen Li ◽  
Zhenzhen Du ◽  
Kun Shi ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Cell Fate ◽  
Zinc Finger ◽  
Oocyte Maturation ◽  
Rna Binding ◽  
Gain Of Function ◽  
Ccch Zinc Finger ◽  
C Complex ◽  
Fate Determinants ◽  
Cell Fate Determinants

During oocyte maturation and the oocyte-to-embryo transition, key developmental regulators such as RNA-binding proteins coordinate translation of particular messenger RNA (mRNAs) and related developmental processes by binding to their cognate maternal mRNAs. In the nematode Caenorhabditis elegans, these processes are regulated by a set of CCCH zinc finger proteins. Oocyte maturation defective-1 (OMA-1) and OMA-2 are two functionally redundant CCCH zinc finger proteins that turnover rapidly during the first embryonic cell division. These turnovers are required for proper transition from oogenesis to embryogenesis. A gain-of-function mutant of OMA-1, oma-1(zu405), stabilizes and delays degradation of OMA-1, resulting in delayed turnover and mis-segregation of other cell fate determinants, which eventually causes embryonic lethality. We performed a large-scale forward genetic screen to identify suppressors of the oma-1(zu405) mutant. We show here that multiple alleles affecting functions of various anaphase promoting complex/cyclosome (APC/C) subunits, including MAT-1, MAT-2, MAT-3, EMB-30, and FZY-1, suppress the gain-of-function mutant of OMA-1. Transcriptome analysis suggested that overall transcription in early embryos occurred after introducing mutations in APC/C genes into the oma-1(zu405) mutant. Mutations in APC/C genes prevent OMA-1 enrichment in P granules and correct delayed degradation of downstream cell fate determinants including pharynx and intestine in excess-1 (PIE-1), posterior segregation-1 (POS-1), muscle excess-3 (MEX-3), and maternal effect germ-cell defective-1 (MEG-1). We demonstrated that only the activator FZY-1, but not FZR-1, is incorporated in the APC/C complex to regulate the oocyte-to-embryo transition. Our findings suggested a genetic relationship linking the APC/C complex and OMA-1, and support a model in which the APC/C complex promotes P granule accumulation and modifies RNA binding of OMA-1 to regulate the oocyte-to-embryo transition process.

scholarly journals Drastic changes in conformational dynamics of the antiterminator M2-1 regulate transcription efficiency in Pneumovirinae

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Cedric Leyrat ◽  
Max Renner ◽  
Karl Harlos ◽  
Juha T Huiskonen ◽  
Jonathan M Grimes
Keyword(s):  
Zinc Finger ◽  
Rna Binding ◽  
Dynamic Equilibrium ◽  
Conformational Dynamics ◽  
Adenosine Monophosphate ◽  
Zinc Finger Domain ◽  
Rna Sequences ◽  
Solution Structures ◽  
Closed Conformation ◽  
Dynamics Simulations

The M2-1 protein of human metapneumovirus (HMPV) is a zinc-binding transcription antiterminator which is highly conserved among pneumoviruses. We report the structure of tetrameric HMPV M2-1. Each protomer features a N-terminal zinc finger domain and an α-helical tetramerization motif forming a rigid unit, followed by a flexible linker and an α-helical core domain. The tetramer is asymmetric, three of the protomers exhibiting a closed conformation, and one an open conformation. Molecular dynamics simulations and SAXS demonstrate a dynamic equilibrium between open and closed conformations in solution. Structures of adenosine monophosphate- and DNA- bound M2-1 establish the role of the zinc finger domain in base-specific recognition of RNA. Binding to ‘gene end’ RNA sequences stabilized the closed conformation of M2-1 leading to a drastic shift in the conformational landscape of M2-1. We propose a model for recognition of gene end signals and discuss the implications of these findings for transcriptional regulation in pneumoviruses.

scholarly journals Recognition of Polyadenosine RNA by the Zinc Finger Domain of Nuclear Poly(A) RNA-binding Protein 2 (Nab2) Is Required for Correct mRNA 3′-End Formation*

2010 ◽  
Vol 285 (34) ◽  
pp. 26022-26032 ◽  
Author(s):  
Seth M. Kelly ◽  
Sara W. Leung ◽  
Luciano H. Apponi ◽  
Anna M. Bramley ◽  
Elizabeth J. Tran ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Zinc Finger Domain

scholarly journals Structural Basis of the Disorder in the Tandem Zinc Finger Domain of the RNA-Binding Protein Tristetraprolin

2016 ◽  
Vol 12 (10) ◽  
pp. 4717-4725 ◽  
Author(s):  
Davide Tavella ◽  
Laura M. Deveau ◽  
Troy W. Whitfield ◽  
Francesca Massi
Keyword(s):  
Zinc Finger ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Structural Basis ◽  
Zinc Finger Domain ◽  
Tandem Zinc Finger

scholarly journals A FYVE zinc finger domain protein specifically links mRNA transport to endosome trafficking

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Thomas Pohlmann ◽  
Sebastian Baumann ◽  
Carl Haag ◽  
Mario Albrecht ◽  
Michael Feldbrügge
Keyword(s):  
Zinc Finger ◽  
Membrane Trafficking ◽  
Molecular Motors ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Detailed Knowledge ◽  
Zinc Finger Domain ◽  
Domain Protein ◽  
Dependent Transport

An emerging theme in cellular logistics is the close connection between mRNA and membrane trafficking. A prominent example is the microtubule-dependent transport of mRNAs and associated ribosomes on endosomes. This coordinated process is crucial for correct septin filamentation and efficient growth of polarised cells, such as fungal hyphae. Despite detailed knowledge on the key RNA-binding protein and the molecular motors involved, it is unclear how mRNAs are connected to membranes during transport. Here, we identify a novel factor containing a FYVE zinc finger domain for interaction with endosomal lipids and a new PAM2-like domain required for interaction with the MLLE domain of the key RNA-binding protein. Consistently, loss of this FYVE domain protein leads to specific defects in mRNA, ribosome, and septin transport without affecting general functions of endosomes or their movement. Hence, this is the first endosomal component specific for mRNP trafficking uncovering a new mechanism to couple mRNPs to endosomes.

scholarly journals A computational study of RNA binding and specificity in the tandem zinc finger domain of TIS11d

2010 ◽  
Vol 19 (6) ◽  
pp. 1222-1234 ◽  
Author(s):  
Brittany R. Morgan ◽  
Francesca Massi
Keyword(s):  
Zinc Finger ◽  
Rna Binding ◽  
Computational Study ◽  
Zinc Finger Domain ◽  
Tandem Zinc Finger
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