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  • 1
    Electronic Resource
    Electronic Resource
    Altered Flagellar Size-Control in shf-1 Short-Flagella Mutants of Chlamydomonas reinhardtii (1984)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 31 (1984), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Two allelic Mendelian mutations which confer a short flagella phenotype were used to explore flagellar size control in Chlamydomonas reinhardtii. When mutant/wild type quadriflagellate dikaryon cells were constructed, their two short flagella rapidly grew out to near wild type length. The kinetics of elongation suggest that the flagellar assembly process is not intrinsically self-limiting as a number of otherwise attractive models for size control require. Instead, we suggest that there exists a cellular machinery dedicated to flagellar size control and that the short-flagella mutations alter the machinery in some as yet unknown way. One of the mutants shows temperature-sensitive flagellar assembly, and both are flagellaless in acetate media. Genetic analysis indicates that the temperaturesensitive, acetate-sensitive, and short-flagella phenotypes have a common genetic basis. The responsible gene has been named shf-1, and it has been mapped to chromosome VI, approximately 5 map units from the centromere.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1984.tb02949.x
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  • 2
    Electronic Resource
    Electronic Resource
    A nuclear suppressor overcomes defects in the synthesis of the chloroplast psbD gene product caused by mutations in two distinct nuclear genes of Chlamydomonas (1995)
    Springer
    Current genetics 27 (1995), S. 263-269 
    Details
    ISSN: 1432-0983
    Keywords: Chloroplast ; Photosystem II ; Chlamydomonas ; Suppression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mutations in two distinct nuclear genes, called NAC 1 and AC-115, of the unicellular green alga Chlamydomonas reinhardtii cause a specific and dramatic reduction in the synthesis of the chloroplast-encoded D2 polypeptide of Photosystem II. The psbD transcript which encodes the D2 protein is present in the mutant strains, but protein pulse-labeling and immunoprecipitation experiments demonstrate that the synthesis of the D2 protein does not occur normally in these cells. These phenotypes are suppressed by an extragenic nuclear suppressor isolated from a pseudorevertant of a nac 1 mutant. This suppressor is neither allele- nor gene-specific in its suppression and is able to overcome the effects of two different mutations in the NAC 1 gene, as well as a mutation in AC-115. The suppressor seems to be specific in its ability to remedy blocks in psbD mRNA translation in the chloroplast. It is not able to restore the translation of another chloroplas-encoded rRNA which is blocked by another nuclear mutation. The suppressor may identify a new nuclear gene specifically involved in the synthesis of the D2 protein in the chloroplast.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00326159
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  • 3
    Electronic Resource
    Electronic Resource
    Cloning and characterization of the nuclear AC115 gene of Chlamydomonas reinhardtii (1999)
    Springer
    Plant molecular biology 39 (1999), S. 1-10 
    Details
    ISSN: 1573-5028
    Keywords: Chlamydomonas ; chloroplast ; D2 protein ; nuclear gene ; photosystem II
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nuclear ac115 mutant of Chlamydomonas reinhardtii is specifically blocked in the synthesis of the chloroplast encoded D2 protein of the photosystem II reaction center at a point after translation initiation. Here, we report the identification of the AC115 gene through complementation rescue of the ac115 mutant strain, using an indexed cosmid library of Chlamydomonas genomic DNA. AC115 is a small, novel, intronless nuclear gene which encodes a protein of 113 amino acids. The amino terminal end of the Ac115 protein is rich in basic amino acids and has features which resemble a chloroplast transit sequence. A hydrophobic stretch of amino acids at the protein's carboxyl terminus is sufficiently large to be a membrane spanning or a protein/protein interaction domain. Various models are discussed to account for the mechanism by which Ac115p works in D2 synthesis. The ac115 mutant allele was sequenced and determined to be an A-to-T transversion at the first position of the fourth codon of the coding sequence. This mutation changes an AAG codon to a TAG nonsense codon and results in a null phenotype.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006108203580
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  • 4
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    A nuclear suppressor overcomes defects in the synthesis of the chloroplast psbD gene product caused by mutations in two distinct nuclear genes of Chlamydomonas (1995)
    Springer
    Details
    Publication Date: 1995-02-01
    Print ISSN: 0172-8083
    Electronic ISSN: 1432-0983
    Topics: Biology
    Published by Springer
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