Molecular Biology and Genetics / Moleküler Biyoloji ve Genetik

Permanent URI for this collectionhttps://hdl.handle.net/11147/9

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  • Article
    Citation - WoS: 17
    Citation - Scopus: 16
    Aggregatibacter Actinomycetemcomitans Groel Protein Promotes Conversion of Human Cd4+ T Cells Into Ifn Gamma Il10 Producing Tbet+ Th1 Cells
    (Public Library of Science, 2012) Saygılı, Tahsin; Akıncılar, Semih Can; Akgül, Bünyamin; Nalbant Aldanmaz, Ayten
    One of the heat shock family protein (Hsp) expressing bacteria is the gram negative, periodontal pathogen Aggregatibacter actinomycetemcomitans (Aa). A. actinomycetemcomitans' Hsp is a 64-kDa GroEL-protein, which has been shown to influence the host cells. In this study we used recombinant A. actinomycetemcomitans GroEL (rAaGroEL) protein as a model antigen to study GroEL-mediated T cell immune response. Human peripheral mononuclear cells (PBMCs), when stimulated with recombinant rAaGroEL, expressed early activation marker CD69 and IL-2R (CD25). CD25 and CD69 expressions were higher in CD4+ T cells compared to CD8+ T cells. rAaGroEL-responding CD4+ T cells expressed IL-10, IFNγ and TNFα cytokines. Interestingly, there were also IL-10 and IFNγ double cytokine producing CD4+ T cells. Additionally, IFNγ expressing CD4+ T cells were also T-bet positive. Altogether the results suggest that rAaGroEL protein affects CD4+ T cells to differentiate into IFNγ IL10-secreting T-bet+ Th1 cells.
  • Article
    Citation - WoS: 50
    Citation - Scopus: 53
    Organization of Carboxysome Genes in the Thiobacilli
    (Springer Verlag, 2003) Cannon, Gordon C.; Baker, Stefanie H.; Soyer Dönmez, Ferda; Johnson, Diana R.; Bradburne, Christopher E.; Mehlman, Jennifer L.; Davies, Paige S.; Jiang, Qinli; Heinhorst, Sabine; Shively, Jessup M.
    The order of genes in the carboxysome gene clusters of four thiobacilli was examined and the possibility of the cluster forming an operon evaluated. Furthermore, carboxysome peptide homologs were compared with respect to similarities in primary sequence, and the unique structural features of the shell protein CsoS2 were described.
  • Article
    Citation - WoS: 90
    Citation - Scopus: 93
    Purification and Characterization of Three Members of the Photolyase/Cryptochrome Family Blue-Light Photoreceptors From Vibrio Cholerae
    (American Society for Biochemistry and Molecular Biology, 2003) Worthington, Erin N.; Kavaklı, İ. Halil; Berrocal-Tito, Gloria M.; Bondo, Bruce; Sancar, Aziz
    The sequence of Vibrio cholerae genome revealed three genes belonging to the photolyase/cryptochrome blue-light photoreceptor family. The proteins encoded by the three genes were purified and characterized. All three proteins contain folate and flavin cofactors and have absorption peaks in the range of 350-500 nm. Only one of the three, VcPhr, is a photolyase specific for cyclobutane pyrimidine dimers. The other two are cryptochromes and were designated VcCry1 and VcCry2, respectively. Mutation of phr abolishes photoreactivation of UV-induced killing, whereas mutations in cry1 and cry2 do not affect photorepair activity. VcCry1 exhibits some unique features. Of all cryptochromes characterized to date, it is the only one that contains stoichiometric amounts of both chromophores and retains its flavin cofactor in the two-electron reduced FADH2 form. In addition, VcCry1 exhibits RNA binding activity and copurifies with an RNA of 60-70 nucleotides in length.