Utilization of stored mRNA during the germination of soybean radicle

2013 ◽  
Vol 30 (1) ◽  
pp. 84-90
Author(s):  
Beixin Mo ◽  
Biao Huang ◽  
Li Liu ◽  
Hao Ye ◽  
Xiaofeng Xu
Keyword(s):  
Stored Mrna

scholarly journals Stored mRNA in sporangiospores of the fungus Mucor racemosus.

1982 ◽  
Vol 150 (3) ◽  
pp. 1138-1144 ◽  
Author(s):  
J E Linz ◽  
M Orlowski
Keyword(s):  
Mucor Racemosus ◽  
Stored Mrna

Molecular cloning of a centrin homolog from Marsilea vestita and evidence for its translational control during spermiogenesis

1999 ◽  
Vol 77 (2) ◽  
pp. 101-108 ◽  
Author(s):  
Peter E Hart ◽  
Stephen M Wolniak
Keyword(s):  
Translational Control ◽  
De Novo ◽  
Basal Bodies ◽  
Motile Cells ◽  
Marsilea Vestita ◽  
Stored Mrna ◽  
Eukaryotic Organisms ◽  
Alpha Amanitin ◽  
Made In

Spermiogenesis in the water fern Marsilea vestita is a process that reaches completion 11 h after dry microspores are immersed in an aqueous medium at 20°C. Each microspore produces 32 spermatozoids and each spermatozoid has a coiled cell body and approximately 140 cilia. The spermatids make basal bodies de novo, from a structure known as a blepharoplast. From the onset of development, the spores contain a large quantity of protein and stored mRNA. We have found previously that centrin, a protein involved in the function of microtubule organizing centers and present in association with basal bodies in motile cells, is made in large quantity approximately 4 h after the microspores are placed into liquid medium. In this paper, we show that a centrin cDNA (MvCen1) we isolated from M. vestita closely resembles centrin cDNAs from other eukaryotic organisms. MvCen1, synthesized in Escherichia coli as a GST-fusion protein, reacted with anti-centrin monoclonal antibodies on immunoblots. Northern blot analysis demonstrates that centrin mRNA is present in the dry microspore at the time of imbibition, at levels that remain constant over 10 h of development and are unaffected by treatment of spores with alpha-amanitin. The centrin transcripts, stored in dry microspores, cannot be translated in vitro for at least 30 min after imbibition.Key words: Marsilea vestita, spermatozoid, spermiogenesis, centrin, MTOC.

scholarly journals Mago Nashi Is Essential for Spermatogenesis in Marsilea

2007 ◽  
Vol 18 (10) ◽  
pp. 3711-3722 ◽  
Author(s):  
Corine M. van der Weele ◽  
Chia-Wei Tsai ◽  
Stephen M. Wolniak
Keyword(s):  
Cell Fate ◽  
De Novo ◽  
Exon Junction Complex ◽  
Protein Distribution ◽  
Stored Mrna ◽  
Asymmetric Divisions ◽  
Core Components ◽  
Conserved Gene ◽  
Tubulin Protein ◽  
Mago Nashi

Spermatogenesis in Marsilea vestita is a rapid process that is activated by placing dry microspores into water. Nine division cycles produce seven somatic cells and 32 spermatids, where size and position define identity. Spermatids undergo de novo formation of basal bodies in a particle known as a blepharoplast. We are interested in mechanisms responsible for spermatogenous initial formation. Mago nashi (Mv-mago) is a highly conserved gene present as stored mRNA and stored protein in the microspore. Mv-mago protein increases in abundance during development and it localizes at discrete cytoplasmic foci (Mago-dots). RNA interference experiments show that new Mv-mago protein is required for development. With Mv-mago silenced, asymmetric divisions become symmetric, cell fate is disrupted, and development stops. The α-tubulin protein distribution, centrin translation, and Mv-PRP19 mRNA distribution are no longer restricted to the spermatogenous cells. Centrin aggregations, resembling blepharoplasts, occur in jacket cells. Mago-dots are undetectable after the silencing of Mv-mago, Mv-Y14, or Mv-eIF4AIII, three core components of the exon junction complex (EJC), suggesting that Mago-dots are either EJCs in the cytoplasm, or Mv-mago protein aggregations dependent on EJCs. Mv-mago protein and other EJC components apparently function in cell fate determination in developing male gametophytes of M. vestita.

scholarly journals Centrin Is Necessary for the Formation of the Motile Apparatus in Spermatids of Marsilea

2001 ◽  
Vol 12 (3) ◽  
pp. 761-776 ◽  
Author(s):  
Vincent P. Klink ◽  
Stephen M. Wolniak
Keyword(s):  
Essential Role ◽  
Normal Development ◽  
De Novo ◽  
Basal Bodies ◽  
Double Stranded Rna ◽  
Rna Probes ◽  
Marsilea Vestita ◽  
Stored Mrna ◽  
Novel Method ◽  
Β Tubulin

During spermiogenesis in the water fern, Marsilea vestita, basal bodies are synthesized de novo in cells that lack preexisting centrioles, in a particle known as a blepharoplast. We have focused on basal body assembly in this organism, asking what components are required for blepharoplast formation. Spermiogenesis is a rapid process that is activated by placing dry microspores into water. Dry microspores contain large quantities of stored protein and stored mRNA, and inhibitors reveal that certain proteins are translated from stored transcripts at specific times during development. Centrin translation accompanies blepharoplast appearance, while β-tubulin translation occurs later, during axonemal formation. In asking whether centrin is an essential component of the blepharoplast, we used antisense, sense, and double-stranded RNA probes made from theMarsilea centrin cDNA, MvCen1, to block centrin translation. We employed a novel method to introduce these RNAs directly into the cells. Antisense and sense both arrest spermiogenesis when blepharoplasts should appear, and dsRNA made from the same cDNA is an effective inhibitor at concentrations at least 10 times lower than either of the single-stranded RNA used in these experiments. Blepharoplasts are undetectable and basal bodies fail to form. Antisense, sense, and dsRNA probes made from Marsileaβ-tubulin permitted normal development until axonemes form. In controls, antisense, sense, and dsRNA, made from a segment of HIV, had no effect on spermiogenesis. Immunoblots suggest that translational blocks induced by centrin-based RNA are gene specific and concentration dependent, since neither β-tubulin- nor HIV-derived RNAs affects centrin translation. The disruption of centrin translation affects microtubule distributions in spermatids, since centrin appears to control formation of the cytoskeleton and motile apparatus. These results show that centrin plays an essential role in the formation of a motile apparatus during spermiogenesis of M. vestita.

S6 ribosomal protein phosphorylation and translation of stored mRNA in maize

Biochimie ◽  
1997 ◽  
Vol 79 (4) ◽  
pp. 187-194 ◽  
Author(s):  
E. Sánchez-de-Jiménez ◽  
R. Aguilar ◽  
T. Dinkova
Keyword(s):  
Ribosomal Protein ◽  
Protein Phosphorylation ◽  
Stored Mrna

245 EFFECT OF BOVINE OOCYTE MATURATION SYSTEM ON RELATIVE ABUNDANCE OF mRNA

2010 ◽  
Vol 22 (1) ◽  
pp. 280
Author(s):  
M. M. Pereira ◽  
F. Q. Costa ◽  
A. P. Oliveira ◽  
C. M. Assunção ◽  
R. V. Serapião ◽  
...  
Keyword(s):  
Relative Abundance ◽  
In Vitro Maturation ◽  
Rna Extraction ◽  
Cumulus Cell ◽  
Sao Paulo ◽  
São Paulo ◽  
Crossbred Cows ◽  
Stored Mrna

The oocyte cytoplasm contains several transcripts that are important for early pre-implantation embryo development, and alterations on the amount of these stored mRNA can disturb oocyte competence. The aim of this study was to evaluate the relative abundance of specific transcripts in oocytes matured in vivo or in vitro. For in vitro maturation, immature oocytes were obtained by ovum pickup from 4 crossbred cows (group 1: G1) or from ovaries collected at a slaughterhouse (group 2: G2) and matured in TCM-199 containing 10% estrus cow serum and 2 μg FSH for 24 h under 5% CO2 in air at 38.5°C. For in vivo maturation, the same crossbred cows used in G1 received a progesterone intravaginal implant (CIDR®, Eazi-Breed CIDRO, São Paulo, Brazil) and 2 mg of estradiol benzoate (Estrogin®, Farmavet, São Paulo, Brazil) on Day 0. On Day 4, cows were superstimulated with 180 mg FSH (Folltropin®, Bioniche, Canada) injected in 6 decreasing doses every 12 h, and on Day 6, the cows received 0.53 mg of sodium cloprostenol (Ciosin®, Cooper, São Paulo, Brazil). On Day 7, CIDR® was removed and 2.5 mg of gonadorelina (Gestran-Plus®, Tecnopec, São Paulo, Brazil) was injected. Ovum pickup was performed 18 h after gonadorelina injection. Oocytes with expanded cumulus cell were then pooled and used as in vivo-matured oocytes (group 3: G3). Oocytes from all groups were denuded and frozen in liquid nitrogen. Pools of 10 oocytes for each group were subject to RNA extraction and reverse transcription. cDNA was amplified by real-time PCR using the beta-actin gene as the endogenous reference. The transcripts analyzed are encoded by TEA domain 2 (TEAD2), high mobility group N1 (HMGN), zygotic arrest 1 (ZAR1), maternal antigen that embryo requires (MATER), growth differentiation factor-9 (GDF9), and peroxiredoxin 1 (PRDX1) genes. Results were analyzed by REST software v.2 using the pair-wise, fixed reallocation randomization test. Data from G3 were used as calibrator. There was no difference (P > 0.05) on relative abundance of all transcripts between pools of oocytes matured in vitro or in vivo obtained from the same cows (G1 and G3, respectively). However, the relative abundance of GDF9 (0.22 ± 0.04-fold) was less (P < 0.05), whereas the relative abundance of TEAD2 transcripts (4.27 ± 2.14-fold) was greater (P < 0.05) for in vitro-matured oocytes obtained from slaugterhouse ovaries (G2) when compared with in vivo-matured oocytes (G3). No difference (P > 0.05) on relative abundance was found between G2 and G3 for the other genes. These data suggest that in vitro maturation does not alter the relative abundance of some transcripts stored into oocytes when compared with the ones stored in oocytes obtained from the same donors by means of multiple ovulation. Financial support was provided by CNPq and FAPEMIG.

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