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  • Wiley  (3)
  • 2010-2014  (3)
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  • Wiley  (3)
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  • 2010-2014  (3)
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  • 1
    Online Resource
    Online Resource
    LIGHT‐INDUCED OIL GLOBULE MIGRATION IN HAEMATOCOCCUS PLUVIALIS (CHLOROPHYCEAE)
    Wiley ; 2012
    In:  Journal of Phycology Vol. 48, No. 5 ( 2012-10), p. 1209-1219
    Details
    In: Journal of Phycology, Wiley, Vol. 48, No. 5 ( 2012-10), p. 1209-1219
    Abstract: Astaxanthin‐rich oil globules in H aematococcus pluvialis display rapid light‐induced peripheral migration that is unique to this organism and serves to protect the photosynthetic system from excessive light. We observed rapid light‐induced peripheral migration that is associated with chlorophyll fluorescence quenching, whereas the recovery was slow. A simple assay to follow globule migration, based on chlorophyll fluorescence level has been developed. Globule migration was induced by high intensity blue light, but not by high intensity red light. The electron transport inhibitor dichlorophenyl‐dimethylurea did not inhibit globule migration, whereas the quinone analog (dibromo‐methyl‐isopropylbenzoquinone), induced globule migration even at low light. Actin microfilament‐directed toxins, such as cytochalasin B and latrunculin A , inhibited the light‐induced globule migration, whereas toxins against microtubules were ineffective. Electron microscopic ( EM ) imaging confirmed the cytoplasmic localization and peripheral migration of globules upon exposure to very high light ( VHL ). Scanning EM of freeze‐fractured cells also revealed globules within cytoplasmic bridges traversing the chloroplast, presumably representing the pathway of migration. Close alignments of globules with endoplasmic reticulum ( ER ) membranes were also observed following VHL illumination. We propose that light‐induced globule migration is regulated by the redox state of the photosynthetic electron transport system. Possible mechanisms of actin‐based globule migration are discussed.
    Type of Medium: Online Resource
    ISSN: 0022-3646 , 1529-8817
    URL: Issue
    URL: Article
    DOI: 10.1111/jpy.2012.48.issue-5
    DOI: 10.1111/j.1529-8817.2012.01210.x
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 2012
    detail.hit.zdb_id: 281226-5
    detail.hit.zdb_id: 1478748-9
    SSG: 12
    Location Call Number Limitation Availability
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  • 2
    Online Resource
    Online Resource
    Cloning and molecular characterization of a novel acyl‐CoA:diacylglycerol acyltransferase 1‐like gene ( PtDGAT1 ) from the diatom Phaeodactylum tricornutum
    Wiley ; 2011
    In:  The FEBS Journal Vol. 278, No. 19 ( 2011-10), p. 3651-3666
    Details
    In: The FEBS Journal, Wiley, Vol. 278, No. 19 ( 2011-10), p. 3651-3666
    Abstract: We have identified and isolated a cDNA encoding a novel acyl‐CoA:diacylglycerol acyltransferase (DGAT)1‐like protein, from the diatom microalga Phaeodactylum tricornutum ( PtDGAT1 ). The full‐length cDNA sequences of PtDGAT1 transcripts revealed that two types of mRNA, PtDGAT1short and PtDGAT1long , were transcribed from the single PtDGAT1 gene. PtDGAT1short encodes a 565 amino acid sequence that is homologous to several functionally characterized higher plant DGAT1 proteins, and 55% identical to the putative DGAT1 of the diatom Thalassiosira pseudonana , but shows little homology with other available putative and cloned algal DGAT sequences. PtDGAT1long lacks several catalytic domains, owing to a 63‐bp nucleotide insertion in the mRNA containing a stop codon. Alternative splicing consisting of intron retention appears to regulate the amount of active DGAT1 produced, providing a possible molecular mechanism for increased triacylglycerol (TAG) biosynthesis in P. tricornutum under nitrogen starvation. DGAT mediates the last committed step in TAG biosynthesis, so we investigated the changes in expression levels of the two types of mRNA following nitrogen starvation inducing TAG accumulation. The abundance of both transcripts was markedly increased under nitrogen starvation, but much less so for PtDGAT1short . PtDGAT1 activity of PtDGAT1short was confirmed in a heterologous yeast transformation system by restoring DGAT activity in a Saccharomyces cerevisiae neutral lipid‐deficient quadruple mutant strain (H1246), resulting in lipid body formation. Lipid body formation was only restored upon the expression of PtDGAT1short , and not of PtDGAT1long . The recombinant yeast appeared to display a preference for incorporating saturated C 16 and C 18 fatty acids into TAG. Database Nucleotide sequence data are available in the GenBank/EMBL/DDBJ databases under accession number HQ589265 , sequence to be released November 15 2011.
    Type of Medium: Online Resource
    ISSN: 1742-464X , 1742-4658
    URL: Issue
    URL: Article
    DOI: 10.1111/ejb.2011.278.issue-19
    DOI: 10.1111/j.1742-4658.2011.08284.x
    Language: English
    Publisher: Wiley
    Publication Date: 2011
    detail.hit.zdb_id: 2172518-4
    SSG: 12
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    Online Resource
  • 3
    Online Resource
    Online Resource
    Isolation of a Novel Oil Globule Protein from the Green Alga Haematococcus pluvialis (Chlorophyceae)
    Wiley ; 2011
    In:  Lipids Vol. 46, No. 9 ( 2011-09), p. 851-861
    Details
    In: Lipids, Wiley, Vol. 46, No. 9 ( 2011-09), p. 851-861
    Abstract: Cytoplasmic oil globules of Haematococcus pluvialis (Chlorophyceae) were isolated and analyzed for pigments, lipids and proteins. Astaxanthin appeared to be the only pigment deposited in the globules. Triacyglycerols were the main lipids (more than 90% of total fatty acids) in both the cell‐free extract and in the oil globules. Lipid profile analysis of the oil globules showed that relative to the cell‐free extract, they were enriched with extraplastidial lipids. A fatty acids profile revealed that the major fatty acids in the isolated globules were oleic acid (18:1) and linoleic acid (18:2). Protein extracts from the globules revealed seven enriched protein bands, all of which were possible globule‐associated proteins. A major 33‐kDa globule protein was partially sequenced by MS/MS analysis, and degenerate DNA primers were prepared and utilized to clone its encoding gene from cDNA extracted from cells grown in a nitrogen depleted medium under high light. The sequence of this 275‐amino acid protein, termed the Haematococcus Oil Globule Protein (HOGP), revealed partial homology with a Chlamydomonas reinhardtii oil globule protein and with undefined proteins from other green algae. The HOGP transcript was barely detectable in vegetative cells, but its level increased by more than 100 fold within 12 h of exposure to nitrogen depletion/high light conditions, which induced oil accumulation. HOGP is the first oil‐globule‐associated protein to be identified in H. pluvialis , and it is a member of a novel gene family that may be unique to green microalgae.
    Type of Medium: Online Resource
    ISSN: 0024-4201 , 1558-9307
    URL: Article
    DOI: 10.1007/s11745-011-3579-4
    Language: English
    Publisher: Wiley
    Publication Date: 2011
    detail.hit.zdb_id: 2030265-4
    SSG: 12
    Location Call Number Limitation Availability
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