A Drosophila gene encoding a DEAD box RNA helicase can suppress loss of wee1/mik1 function in Schizosaccharomyces pombe

1994 ◽  
Vol 245 (5) ◽  
pp. 654-657 ◽  
Author(s):  
Emma Warbrick ◽  
David Glover
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Rna Helicase ◽  
Gene Encoding ◽  
Drosophila Gene ◽  
Dead Box

A yeast gene encoding a putative RNA helicase of the “DEAD”-box family

Yeast ◽  
1993 ◽  
Vol 9 (4) ◽  
pp. 429-432 ◽  
Author(s):  
Sabine Strahl-Bolsinger ◽  
Widmar Tanner
Keyword(s):  
Rna Helicase ◽  
Yeast Gene ◽  
Gene Encoding ◽  
Dead Box ◽  
The Dead

scholarly journals The DEAD box RNA helicase Ddx39a is essential for myocyte and lens development in zebrafish

2017 ◽  
Author(s):  
Linlin Zhang ◽  
Beibei Li ◽  
Yuxi Yang ◽  
Ian C. Scott ◽  
Xin Lou
Keyword(s):  
Heart Development ◽  
Rna Helicase ◽  
Lens Fiber ◽  
Rna Helicases ◽  
Gene Encoding ◽  
Animal Development ◽  
Fiber Cells ◽  
Dead Box ◽  
The Dead ◽  
Almost All

AbstractRNA helicases from the DEAD-box family are found in almost all organisms and have important roles in RNA metabolism including RNA synthesis, processing and degradation. The function and mechanism of action of most of these helicases in animal development and human disease are largely unexplored. In a zebrafish mutagenesis screen to identify genes essential for heart development we identified a zebrafish mutant, which disrupts the gene encoding the RNA helicase DEAD-box 39a (ddx39a).Homozygous ddx39a mutant embryos exhibit profound cardiac and trunk muscle dystrophy, along with lens abnormalities caused by abrupt terminal differentiation of cardiomyocyte, myoblast and lens fiber cells. Further investigation indicated that loss of ddx39a hindered mRNA splicing of members of the kmt2 gene family, leading to mis-regulation of structural gene expression in cardiomyocyte, myoblast and lens fiber cells. Taken together, these results show that Ddx39a plays an essential role in establishment of proper epigenetic status during cell differentiation.

scholarly journals RNA helicase–regulated processing of the Synechocystis rimO–crhR operon results in differential cistron expression and accumulation of two sRNAs

2020 ◽  
Vol 295 (19) ◽  
pp. 6372-6386 ◽  
Author(s):  
Albert Remus R. Rosana ◽  
Denise S. Whitford ◽  
Anzhela Migur ◽  
Claudia Steglich ◽  
Sonya L. Kujat-Choy ◽  
...  
Keyword(s):  
Small Rnas ◽  
Rna Helicase ◽  
Rnase E ◽  
Gene Encoding ◽  
Modeling And Analysis ◽  
Dead Box ◽  
Bacterial Rna ◽  
Additional Processing ◽  
Operon Expression

The arrangement of functionally-related genes in operons is a fundamental element of how genetic information is organized in prokaryotes. This organization ensures coordinated gene expression by co-transcription. Often, however, alternative genetic responses to specific stress conditions demand the discoordination of operon expression. During cold temperature stress, accumulation of the gene encoding the sole Asp–Glu–Ala–Asp (DEAD)-box RNA helicase in Synechocystis sp. PCC 6803, crhR (slr0083), increases 15-fold. Here, we show that crhR is expressed from a dicistronic operon with the methylthiotransferase rimO/miaB (slr0082) gene, followed by rapid processing of the operon transcript into two monocistronic mRNAs. This cleavage event is required for and results in destabilization of the rimO transcript. Results from secondary structure modeling and analysis of RNase E cleavage of the rimO–crhR transcript in vitro suggested that CrhR plays a role in enhancing the rate of the processing in an auto-regulatory manner. Moreover, two putative small RNAs are generated from additional processing, degradation, or both of the rimO transcript. These results suggest a role for the bacterial RNA helicase CrhR in RNase E-dependent mRNA processing in Synechocystis and expand the known range of organisms possessing small RNAs derived from processing of mRNA transcripts.

scholarly journals The Drosophila gene abstrakt, required for visual system development, encodes a putative RNA helicase of the DEAD box protein family

2000 ◽  
Vol 91 (1-2) ◽  
pp. 189-196 ◽  
Author(s):  
Dietmar Schmucker ◽  
Gerd Vorbrüggen ◽  
Paula Yeghiayan ◽  
Hong Qing Fan ◽  
Herbert Jäckle ◽  
...  
Keyword(s):  
Visual System ◽  
System Development ◽  
Rna Helicase ◽  
Protein Family ◽  
Drosophila Gene ◽  
Dead Box ◽  
The Dead ◽  
Visual System Development

scholarly journals Rok1p is a putative RNA helicase required for rRNA processing.

1997 ◽  
Vol 17 (6) ◽  
pp. 3398-3407 ◽  
Author(s):  
J Venema ◽  
C Bousquet-Antonelli ◽  
J P Gelugne ◽  
M Caizergues-Ferrer ◽  
D Tollervey
Keyword(s):  
18S Rrna ◽  
Synthetic Lethality ◽  
Rna Helicase ◽  
Rrna Synthesis ◽  
Temperature Sensitive ◽  
Rrna Processing ◽  
Gene Encoding ◽  
Dead Box ◽  
Rrna Cleavage ◽  
Cleavage Reactions

The synthesis of ribosomes involves many small nucleolar ribonucleoprotein particles (snoRNPs) as transacting factors. Yeast strains lacking the snoRNA, snR10, are viable but are impaired in growth and delayed in the early pre-rRNA cleavages at sites A0, A1, and A2, which lead to the synthesis of 18S rRNA. The same cleavages are inhibited by genetic depletion of the essential snoRNP protein Gar1p. Screens for mutations showing synthetic lethality with deletion of the SNR10 gene or with a temperature-sensitive gar1 allele both identified the ROK1 gene, encoding a putative, ATP-dependent RNA helicase of the DEAD-box family. The ROK1 gene is essential for viability, and depletion of Rok1p inhibits pre-rRNA processing at sites A0, A1, and A2, thereby blocking 18S rRNA synthesis. Indirect immunofluorescence by using a ProtA-Rok1p construct shows the protein to be predominantly nucleolar. These results suggest that Rok1p is required for the function of the snoRNP complex carrying out the early pre-rRNA cleavage reactions.

scholarly journals A second maternally expressed Drosophila gene encodes a putative RNA helicase of the "DEAD box" family.

1991 ◽  
Vol 88 (6) ◽  
pp. 2113-2117 ◽  
Author(s):  
T. de Valoir ◽  
M. A. Tucker ◽  
E. J. Belikoff ◽  
L. A. Camp ◽  
C. Bolduc ◽  
...  
Keyword(s):  
Rna Helicase ◽  
Drosophila Gene ◽  
Dead Box ◽  
The Dead

scholarly journals The Schizosaccharomyces pombe cho1+ Gene Encodes a Phospholipid Methyltransferase

Genetics ◽  
1998 ◽  
Vol 150 (2) ◽  
pp. 553-562
Author(s):  
Margaret I Kanipes ◽  
John E Hill ◽  
Susan A Henry
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Sequence Analysis ◽  
Schizosaccharomyces Pombe ◽  
Gene Disruption ◽  
Structure And Function ◽  
Biosynthetic Enzyme ◽  
Gene Encoding ◽  
Complementation Groups ◽  
Eukaryotic Organisms ◽  
And Function

Abstract The isolation of mutants of Schizosaccharomyces pombe defective in the synthesis of phosphatidylcholine via the methylation of phosphatidylethanolamine is reported. These mutants are choline auxotrophs and fall into two unlinked complementation groups, cho1 and cho2. We also report the analysis of the cho1+ gene, the first structural gene encoding a phospholipid biosynthetic enzyme from S. pombe to be cloned and characterized. The cho1+ gene disruption mutant (cho1Δ) is viable if choline is supplied and resembles the cho1 mutants isolated after mutagenesis. Sequence analysis of the cho1+ gene indicates that it encodes a protein closely related to phospholipid methyltransferases from Saccharomyces cerevisiae and rat. Phospholipid methyltransferases encoded by a rat liver cDNA and the S. cerevisiae OPI3 gene are both able to complement the choline auxotrophy of the S. pombe cho1 mutants. These results suggest that both the structure and function of the phospholipid N-methyltransferases are broadly conserved among eukaryotic organisms.

scholarly journals Association of the Cold Shock DEAD-Box RNA Helicase RhlE to the RNA Degradosome in Caulobacter crescentus

2017 ◽  
Vol 199 (13) ◽  
Author(s):  
Angel A. Aguirre ◽  
Alexandre M. Vicente ◽  
Steven W. Hardwick ◽  
Daniela M. Alvelos ◽  
Ricardo R. Mazzon ◽  
...  
Keyword(s):  
Low Temperature ◽  
Caulobacter Crescentus ◽  
Immunoblot Analysis ◽  
Rna Helicase ◽  
Rnase E ◽  
Rna Helicases ◽  
Content Type ◽  
Dead Box ◽  
Rna Degradosome ◽  
The Dead

ABSTRACT In diverse bacterial lineages, multienzyme assemblies have evolved that are central elements of RNA metabolism and RNA-mediated regulation. The aquatic Gram-negative bacterium Caulobacter crescentus, which has been a model system for studying the bacterial cell cycle, has an RNA degradosome assembly that is formed by the endoribonuclease RNase E and includes the DEAD-box RNA helicase RhlB. Immunoprecipitations of extracts from cells expressing an epitope-tagged RNase E reveal that RhlE, another member of the DEAD-box helicase family, associates with the degradosome at temperatures below those optimum for growth. Phenotype analyses of rhlE, rhlB, and rhlE rhlB mutant strains show that RhlE is important for cell fitness at low temperature and its role may not be substituted by RhlB. Transcriptional and translational fusions of rhlE to the lacZ reporter gene and immunoblot analysis of an epitope-tagged RhlE indicate that its expression is induced upon temperature decrease, mainly through posttranscriptional regulation. RNase E pulldown assays show that other proteins, including the transcription termination factor Rho, a second DEAD-box RNA helicase, and ribosomal protein S1, also associate with the degradosome at low temperature. The results suggest that the RNA degradosome assembly can be remodeled with environmental change to alter its repertoire of helicases and other accessory proteins. IMPORTANCE DEAD-box RNA helicases are often present in the RNA degradosome complex, helping unwind secondary structures to facilitate degradation. Caulobacter crescentus is an interesting organism to investigate degradosome remodeling with change in temperature, because it thrives in freshwater bodies and withstands low temperature. In this study, we show that at low temperature, the cold-induced DEAD-box RNA helicase RhlE is recruited to the RNA degradosome, along with other helicases and the Rho protein. RhlE is essential for bacterial fitness at low temperature, and its function may not be complemented by RhlB, although RhlE is able to complement for rhlB loss. These results suggest that RhlE has a specific role in the degradosome at low temperature, potentially improving adaptation to this condition.

Sign in / Sign up

Export Citation Format

Share Document