Evidence for an association between U1 RNA and interspersed repeat single-copy RNAs in the cytoplasm of sea urchin eggs

Development ◽  
1987 ◽  
Vol 101 (1) ◽  
pp. 107-116
Author(s):  
S. Ruzdijic ◽  
T. Pederson
Keyword(s):  
Sea Urchin ◽  
Messenger Rna ◽  
Single Copy ◽  
Mrna Splicing ◽  
Rna Molecules ◽  
Sea Urchin Egg ◽  
Selection Experiments ◽  
U1 Snrnp ◽  
Egg Extracts ◽  
Rna Complexes

Psoralen crosslinking of RNA-RNA intermolecular duplexes in sea urchin egg extracts reveals that some maternal poly(A)+ RNA molecules are complexed with U1 RNA, a cofactor in somatic nuclear pre-mRNA splicing. Reaction of egg extracts with a monoclonal antibody specific for U1 snRNP selects, in addition to U1, RNAs that contain repeated sequences interspersed with single-copy elements. Antibody-selection experiments with nucleate and anucleate egg halves demonstrate that most of the U1 RNA-interspersed RNA complexes are cytoplasmic, as is the egg's store of total U1 snRNP. These results raise the possibility that maternal interspersed RNAs include unprocessed pre-messenger RNA molecules in arrested complexes with splicing cofactors.

scholarly journals Phylogenetic comparison and splice site conservation of eukaryotic U1 snRNP-specific U1-70K gene family

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tao Fan ◽  
Yu-Zhen Zhao ◽  
Jing-Fang Yang ◽  
Qin-Lai Liu ◽  
Yuan Tian ◽  
...  
Keyword(s):  
Gene Family ◽  
Splice Site ◽  
Messenger Rna ◽  
Expression Patterns ◽  
Protein Structures ◽  
Single Copy ◽  
Central Component ◽  
Animal Kingdom ◽  
Functional Studies ◽  
U1 Snrnp

AbstractEukaryotic cells can expand their coding ability by using their splicing machinery, spliceosome, to process precursor mRNA (pre-mRNA) into mature messenger RNA. The mega-macromolecular spliceosome contains multiple subcomplexes, referred to as small nuclear ribonucleoproteins (snRNPs). Among these, U1 snRNP and its central component, U1-70K, are crucial for splice site recognition during early spliceosome assembly. The human U1-70K has been linked to several types of human autoimmune and neurodegenerative diseases. However, its phylogenetic relationship has been seldom reported. To this end, we carried out a systemic analysis of 95 animal U1-70K genes and compare these proteins to their yeast and plant counterparts. Analysis of their gene and protein structures, expression patterns and splicing conservation suggest that animal U1-70Ks are conserved in their molecular function, and may play essential role in cancers and juvenile development. In particular, animal U1-70Ks display unique characteristics of single copy number and a splicing isoform with truncated C-terminal, suggesting the specific role of these U1-70Ks in animal kingdom. In summary, our results provide phylogenetic overview of U1-70K gene family in vertebrates. In silico analyses conducted in this work will act as a reference for future functional studies of this crucial U1 splicing factor in animal kingdom.

Chapter 9 Actin Gelation in Sea Urchin Egg Extracts

1982 ◽  
pp. 175-199 ◽  
Author(s):  
Joseph Bryan ◽  
Robert E. Kane
Keyword(s):  
Sea Urchin ◽  
Sea Urchin Egg ◽  
Egg Extracts

The mobilization of maternal histone messenger RNA after fertilization of the sea urchin egg

1978 ◽  
Vol 7 (1-2) ◽  
pp. 103-114 ◽  
Author(s):  
D.E. Woods ◽  
W. Fitschen
Keyword(s):  
Sea Urchin ◽  
Messenger Rna ◽  
Sea Urchin Egg

ANGEL2 is a member of the CCR4 family of deadenylases with 2′,3′-cyclic phosphatase activity

Science ◽  
2020 ◽  
Vol 369 (6503) ◽  
pp. 524-530
Author(s):  
Paola H. Pinto ◽  
Alena Kroupova ◽  
Alexander Schleiffer ◽  
Karl Mechtler ◽  
Martin Jinek ◽  
...  
Keyword(s):  
Messenger Rna ◽  
De Novo ◽  
Mrna Splicing ◽  
Rna Molecules ◽  
Unfolded Protein ◽  
Rna Pathways ◽  
The Unfolded Protein Response ◽  
Protein Response ◽  
Cyclic Phosphates ◽  
Hydrolysis Of

RNA molecules are frequently modified with a terminal 2′,3′-cyclic phosphate group as a result of endonuclease cleavage, exonuclease trimming, or de novo synthesis. During pre-transfer RNA (tRNA) and unconventional messenger RNA (mRNA) splicing, 2′,3′-cyclic phosphates are substrates of the tRNA ligase complex, and their removal is critical for recycling of tRNAs upon ribosome stalling. We identified the predicted deadenylase angel homolog 2 (ANGEL2) as a human phosphatase that converts 2′,3′-cyclic phosphates into 2′,3′-OH nucleotides. We analyzed ANGEL2’s substrate preference, structure, and reaction mechanism. Perturbing ANGEL2 expression affected the efficiency of pre-tRNA processing, X-box–binding protein 1 (XBP1) mRNA splicing during the unfolded protein response, and tRNA nucleotidyltransferase 1 (TRNT1)–mediated CCA addition onto tRNAs. Our results indicate that ANGEL2 is involved in RNA pathways that rely on the ligation or hydrolysis of 2′,3′-cyclic phosphates.

Identification of MAPKAPK Homolog (MAPKAPK-4) as a Myosin II Regulatory Light-Chain Kinase in Sea Urchin Egg Extracts

1997 ◽  
Vol 343 (1) ◽  
pp. 55-62 ◽  
Author(s):  
Satoshi Komatsu ◽  
Norio Murai ◽  
Go Totsukawa ◽  
Mari Abe ◽  
Koji Akasaka ◽  
...  
Keyword(s):  
Sea Urchin ◽  
Light Chain ◽  
Myosin Ii ◽  
Regulatory Light Chain ◽  
Sea Urchin Egg ◽  
Egg Extracts

scholarly journals Actin polymerization and interaction with other proteins in temperature-induced gelation of sea urchin egg extracts.

1976 ◽  
Vol 71 (3) ◽  
pp. 704-714 ◽  
Author(s):  
R E Kane
Keyword(s):  
Sea Urchin ◽  
Low Temperatures ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
Complex Structure ◽  
The Other ◽  
Cytoplasmic Proteins ◽  
Sea Urchin Egg ◽  
Low Concentrations ◽  
Egg Extracts

The gel which forms on warming the extracts of the cytoplasmic proteins of sea urchin eggs has been separated into two fractions, one containing F-actin and the other containing two proteins of 58,000 and 22,000 mol wt. When combined in 0.1 M KCl, even at 0 degrees C, these components will form gel material identical to that formed by warming extracts. This gel is a network of laterally aggregated F-actin filaments which are in register and which display a complex cross-banding pattern generated by the presence of the other two proteins. Low concentrations of calcium block the assembly of these proteins to form this complex structure, which may play some cytoskeletal role in the cytoplasm. This association of F-actin with the other proteins to form a gel is very likely the last step fo the process occurring in warmed extracts. At low temperatures, gelation of extracts is limited by the relative absence of F-actin, as demonstrated by the inability to sediment it at 100,000 g and also by the fact that gelation occurs immediately if exogenous F-actin is added to cold extracts. The transformation of the G-actin present in the extract to the F-form is apparently repressed at low temperatures. This is shown directly by the failure of added G-actin to polymerize at low temperatures in the presence of extract. These observations resemble those which have been reported on preparations from amoeboid cells and may be significant in the involvement of actin and these other proteins in cell division and later developmental processes.

scholarly journals STABILITIES OF NUCLEAR AND MESSENGER RNA MOLECULES IN SEA URCHIN EMBRYOS

1972 ◽  
Vol 53 (2) ◽  
pp. 474-482 ◽  
Author(s):  
Bruce P. Brandhorst ◽  
Tom Humphreys
Keyword(s):  
Steady State ◽  
Sea Urchin ◽  
Half Life ◽  
Messenger Rna ◽  
Cell Fractionation ◽  
Rna Molecules ◽  
Sea Urchin Embryos ◽  
Cytoplasmic Rna ◽  
Nuclear Rna ◽  
Kinetics Of

The kinetics of accumulation of radioactive adenosine in adenosine triphosphate and in RNA of nuclear, cytoplasmic, and polysomal fractions of sea urchin embryos have been analyzed. 85% of the RNA synthesized decays in the nucleus with an apparently uniform half-life of about 7 min. The remaining 15% goes to the cytoplasm, mostly entering polysomes, and decays with a quite uniform half-life of about 75 min. The nuclear RNA accounts for one-third and the cytoplasmic RNA accounts for two-thirds of the total unstable RNA which accumulates at steady state in the embryo. The size distribution of short-labeled nuclear RNA is very similar to that of long-labeled messenger RNA, when both are extracted directly from the cells without a previous cell fractionation.

scholarly journals Preparation and purification of polymerized actin from sea urchin egg extracts.

1975 ◽  
Vol 66 (2) ◽  
pp. 305-315 ◽  
Author(s):  
R E Kane
Keyword(s):  
Sea Urchin ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Mammalian Brain ◽  
Simple Method ◽  
Cytoplasmic Proteins ◽  
Sea Urchin Egg ◽  
Egg Extracts ◽  
Low Levels ◽  
Birefringent Fibrils

Isotonic extracts of the soluble cytoplasmic proteins of sea urchin eggs, containing sufficient EGTA to reduce the calcium concentration to low levels, form a dense gel on warming to 35-40 degrees C. Although this procedure is similar to that used to polymerize tubulin from mammalian brain, sodium dodecyl sulfate-polyacrylamide gel electrophoresis shows this gel to have actin as a major component and to contain no tubulin. If such extracts are dialyzed against dilute salt solution, they no longer respond to warming, but gelation will occur if they are supplemented with 1 mM ATP and 0.020 M KCl before heating. Gelation is not temperature reversible, but the gelled material can be dissolved in 0.6-1 M KCl and these solutions contain F-actin filaments. These filaments slowly aggregate to microscopic, birefringent fibrils when 1 mM ATP is added to the solution, and this procedure provides a simple method for preparing purified actin. the supernate remaining after actin removal contains the other two components of the gel, proteins of approximately 58,000 and 220,000 mol wt. These two proteins plus actin recombine to form the original gel material when the ionic strength is reduced. This reaction is reversible at 0 degrees C, and no heating is required.

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