Gossypium hirsutum
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ABSTRACT:
PROVIDER: PRJNA93611 | ENA |
REPOSITORIES: ENA
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Project description:Cotton Fiber Development Time-course Analysis
| PRJNA104531 | ENA
Project description:We explored the transcriptomic alterations associated with domestication by interrogating a developmental time course of cotton fibers from the wild G. hirsutum var. yucatanense and a representative of an elite domesticated line.
2010-12-22 | GSE23517 | GEO
Project description:DP16 ovules of -4, -2, 2 dpa compared to 0 dpa Keywords: Time Course
2005-11-03 | GSE3545 | GEO
Project description:We explored the transcriptomic alterations associated with domestication by interrogating a developmental time course of cotton fibers from the wild G. hirsutum var. yucatanense and a representative of an elite domesticated line. 30 chip design - including 2 species (wild and domesticated cotton), by 1 tissue (fiber), for 5 timepoints (2,7,10,20, and 25 days after anthesis), with 3 replicates per timepoint
2010-12-22 | E-GEOD-23517 | biostudies-arrayexpress
Project description:As part of our research on peroxisome biogenesis, catalase was purified from cotyledons of dark-grown cotton (Gossypium hirsutum L.) seedlings and monospecific antibodies were raised in rabbits. Purified catalase appeared as three distinct electrophoretic forms in non-denaturing gels and as a single protein band (with a subunit Mr of 57,000) on silver-stained SDS/polyacrylamide gels. Western blots of crude extracts and isolated peroxisomes from cotton revealed one immunoreactive polypeptide with the same Mr (57,000) as the purified enzyme, indicating that catalase did not undergo any detectable change in Mr during purification. Synthesis in vitro, directed by polyadenylated RNA isolated from either maturing seeds or cotyledons of dark-grown cotton seedlings, revealed a predominant immunoreactive translation product with a subunit Mr of 57,000 and an additional minor immunoreactive product with a subunit Mr of 64000. Labelling studies in vivo revealed newly synthesized monomers of both the 64000- and 57,000-Mr proteins present in the cytosol and incorporation of both proteins into the peroxisome without proteolytic processing. Within the peroxisome, the 57,000-Mr catalase was found as an 11S tetramer; whereas the 64,000-Mr protein was found as a relatively long-lived 20S aggregate (native Mr approx. 600,000-800,000). The results strongly indicate that the 64,000-Mr protein (catalase?) is not a precursor to the 57,000-Mr catalase and that cotton catalase is translated on cytosolic ribosomes without a cleavable transit or signal sequence.
| S-EPMC1148976 | biostudies-other
Project description:We conduct a genome-wide analysis of the DNA sequences associated with CenH3 using chromatin immunoprecipitation to map the position of centromere regions.
2019-01-17 | GSE119184 | GEO
Project description:In order to study gene expression at the genomic level during elongation and secondary cell wall synthesis of upland cotton fiber, oligonucleotide microarrays were employed. RNA was isolated from fibers in 7 different time points beginning prior to peak fiber expansion, continuing through termination of fiber expansion and ending at peak cellulose synthesis (5, 8, 10, 14, 17, 21, and 24dpa). The arrays contained ~25,000 oligonucleotides representing ~12,200 genes designed from a fiber EST database during peak cell expansion. Dynamic changes in gene expression were analyzed in a developmental context to identify stage-specific biological processes and pathways likely to be crucial to cell polar elongation or cellulose biosynthesis and secondary cell wall biogenesis. Genes with significant changes in expression relative to any preceding time point were identified (moderated t-statistics, adjusted p-value <0.05) for each developmental time point with an expected false discovery rate for multiple testing <5%
2008-06-12 | GSE11693 | GEO
Project description:Low dosages of chloramphenicol (25-50 micrograms/ml) brought about a 2-4-fold stimulation of acid phosphatase activity in 48 h-germinated cotton (Gossypium hirsutum) embryos. However, at high concentrations of chloramphenicol (100-1000 micrograms/ml), there was a progressive decline in enzyme activity. The stimulatory effect of the drug on acid phosphatase activity was relatively specific, since no significant stimulation of activities of proteinase, deoxyribonuclease, ribonuclease, o-diphenolase and peroxidase was observed in germinating cotton embryos. Chloramphenicol, however, did promote the activities of isocitric lyase and alkaline phosphatase. Sephadex G-200 chromatography of the enzyme fraction revealed high (230 000)- and low (106 000)-molecular-weight multiple forms of acid phosphatase in the chloramphenicol-treated embryos, in contrast with a single molecular form (mol.wt. 106 000) in the untreated embryos. Thus the treatment of cotton embryos with chloramphenicol induced both a qualitative and a quantitative change in the acid phosphatase activity. Chloramphenicol-stimulated acid phosphatase activity was strongly inhibited when Pi was included in the germination medium. However, the control embryos showed less pronounced inhibition of enzyme activity in presence of Pi ions.
| S-EPMC1152011 | biostudies-other