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  • 1
    Digitale Medien
    Digitale Medien
    The Aspergillus nidulans sldIRAD50 gene interacts with bimEAPC1, a homologue of an anaphase-promoting complex subunit (2005)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 57 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie , Medizin
    Notizen: The Mre11–Rad50–Nbs1 protein complex has emerged as a central component in the human cellular DNA damage response, and recent observations suggest that these proteins are at least partially responsible for the linking of DNA damage detection to DNA repair and cell cycle checkpoint functions. We have identified Aspergillus nidulans sldI1444D mutant in a screen for dynein synthetic lethals. The sldIRAD50 gene was cloned by complementation of the sporulation deficiency phenotype of this mutant. A transversion G→C at the position 2509 (Ala-692-Pro amino acid change) in the sldI1444D mutant causes sensitivity to several DNA-damaging agents. The mutation sldI1 occurs at the CXXC hinge domain of Rad50. We have deleted part of the coiled-coil and few amino acids of the Rad50–Mre11 interaction region and assessed several phenotypic traits in this deletion strain. Besides sensitivity to a number of DNA-damaging agents, this deletion strain is also impaired in the DNA replication checkpoint response, and in ascospore viability. There is no delay of the S-phase when germlings of both sldI RAD50 and mreAMRE11 inactivation strains were exposed to the DNA damage caused by bleomycin. Transformation experiments and Southern blot analysis indicate homologous recombination is dependent on scaANBS1 function in the Mre11 complex. There are epistatic and synergistic interactions between sldI RAD50 and bimEAPC1 at S-phase checkpoints and response to hydroxyurea and UV light. Our results suggest a possible novel feature of the Mre11 complex in A. nidulans, i.e. a relationship with bimE APC1.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-2958.2005.04671.x
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  • 2
    Digitale Medien
    Digitale Medien
    Isolation of a new set of Aspergillus nidulans mutants defective in nuclear migration (1999)
    Springer
    Current genetics 35 (1999), S. 626-630 
    Details
    ISSN: 1432-0983
    Schlagwort(e): Key wordsA. nidulans ; Arp1 ; Cytoplasmic dynein ; Nuclear migration
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract In the filamentous fungus Aspergillus nidulans, nuclear migration in the germ tube is mediated by cytoplasmic dynein. We have previously reported the characterization of four nud (nuclear distribution) genes, nudA, nudC, nudF and nudG, involved in this process. The nudA and nudG genes respectively encode for the heavy chain and the 8-kDa light chain of cytoplasmic dynein. In this work, we describe an improved method for the isolation of nud mutants that has led to the identification of at least ten additional nud loci. We have cloned one of the genes, nudK, and determined that it encodes the actin-related protein Arp1, which is a component of the dynactin complex. This provides the first evidence that dynactin is involved in nuclear migration in A. nidulans.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s002940050461
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  • 3
    Digitale Medien
    Digitale Medien
    Bacteriophage T4 as a surface display vector (1995)
    Springer
    Virus genes 10 (1995), S. 173-177 
    Details
    ISSN: 1572-994X
    Schlagwort(e): bacteriophage T4 ; fibritin ; surface display vector ; homologous recombination ; HBV
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract We describe a method for construction of hymeric bacteriophage T4 particles displaying foreign polypeptides on their surface. The method is based on our finding that minor T4 fibrous protein fibritin encoded by genewac (whisker's antigen control) could be lengthened at the C terminus without impairing its folding or binding to the phage particle. The lengthened fibritin gene could easily be transferred into the T4 genome by homologous recombination with a plasmid containing the modified genewac. The modified genewac is expressed properly during phage reproduction, and the lengthened fibritin is bound to phage particles. As an example of this type of method, we have obtained the hymeric T4 particles carrying a polypeptide of 53 residues, 45 of which are from the pre-S2 region of hepatitis B virus. The T4 display vector extends currently available display systems.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01702598
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  • 4
    Digitale Medien
    Digitale Medien
    Crystallization and preliminary crystallographic study of the pentamerizing domain from cartilage oligomeric matrix protein: A five-stranded α-helical bundle (1996)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 24 (1996), S. 259-262 
    Details
    ISSN: 0887-3585
    Schlagwort(e): coiled-coil ; extracellular matrix ; thrombospondin ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: Cartilage oligomeric matrix protein (COMP) is a pentameric glycoprotein of the thrombospondin family found in cartilage and tendon. Self-association of COMP is achieved through the formation of a five-stranded α-helical bundle that involves 64 N-terminal residues (from 20 to 83). The complex is further stabilized by the interchain disulfide bonds between cysteines 68 and 71. We have prepared, by expression in Escherichia coli, several peptides of different lengths from the N-terminal region of COMP and studied their amenability to crystallization. Crystals of the best quality were obtained with a peptide spanning COMP residues 28-72. This peptide forms disulfide linked pentamers with 87% of α-helical structure. Crystals were grown by the hanging drop vapor diffusion method, using polyethylene glycol 1500 as a precipitant. The crystals belong to space group P21 with unit cell dimensions a = 38.47 Å, b = 49.47 Å, c = 54.98 Å, β = 103.84° and contain one pentamer per asymmetric unit. They diffract strongly to at least 1.8 Å resolution.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
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