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Full-Text Articles in Molecular Biology

Genetic Construction And Biochemical Analysis Of Thermostability Mutants Of Glucoamylase From Aspergillus Awamori , Yuxing Li Jan 1996

Genetic Construction And Biochemical Analysis Of Thermostability Mutants Of Glucoamylase From Aspergillus Awamori , Yuxing Li

Retrospective Theses and Dissertations

To study the molecular basis of Aspergillus awamori glucoamylase (GA) thermostability, eighteen mutants were constructed by site-directed mutagenesis and expressed in Saccharomyces cerevisiae based on thermostability theories. Four lysine residues, K61, K279, K352 and K404, were replaced with arginine, with all but K404 well exposed to the solvent and far away from the enzyme activity site. Mutations K61F/D65E and H254W/E326Q were made to fill a packing void around the inner set of six [alpha]-helices of GA and to displace water molecules inside the void. Five residues (A27, A393, A435, Ser436 and Ser460) were replaced with proline. Two ...


Molecular Characterization Of The Chloroplastic Acetyl-Coa Carboxylase Of Arabidopsis Thaliana , Joong-Kook Choi Jan 1996

Molecular Characterization Of The Chloroplastic Acetyl-Coa Carboxylase Of Arabidopsis Thaliana , Joong-Kook Choi

Retrospective Theses and Dissertations

Acetyl-CoA carboxylase (ACCase) is a biotin-containing enzyme that catalyzes the formation of malonyl-CoA from acetyl-CoA. Dicot plants such as Arabidopsis contain two structurally distinct types of ACCases that are located in different subcellular compartments. The ACCase located in the cytosol of plant cells generates malonyl-CoA for the synthesis of plant secondary metabolites, including a variety of polyketides and derivatives, and malonylated phytochemicals. The ACCase that is located in chloroplasts generates malonyl-CoA for de novo fatty acid biosynthesis. This enzyme has a heteromeric structure consisting of at least four subunits: the biotin-carrier subunit, coded by the CAC1 gene, the biotin carboxylase ...


Integration Specificity Of The Retrovirus-Like Transposable Element Ty5 Of Saccharomyces , Sige Zou Jan 1996

Integration Specificity Of The Retrovirus-Like Transposable Element Ty5 Of Saccharomyces , Sige Zou

Retrospective Theses and Dissertations

The retrotransposons and retroviruses display a strong preference in selecting integration sites. The molecular mechanisms underlying this process, however, are largely unknown. I have characterized a new retrotransposon, called Ty5, in diverse strains of Saccharomyces cerevisiae and related species. A functional element, Ty5-6p, was identified from S. paradoxus. To investigate Ty5 target preference, the locations of 13 native insertions were determined in S. cerevisiae and S. paradoxus. Twelve were found near the telomeres and the mating locus HMR. To determine if this distribution is a consequence of targeted integration, a Ty5 transposition assay was developed in S. cerevisiae using Ty5-6p ...