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Silja Kuusk
University of Tartu
10Publications
8H-index
190Citations
Publications 10
Newest
#1Silja Kuusk (UT: University of Tartu)H-Index: 8
#2Riin KontH-Index: 4
Last.Priit VäljamäeH-Index: 19
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4 CitationsSource
#1Silja Kuusk (UT: University of Tartu)H-Index: 8
#2Bastien Bissaro (NMBU: Norwegian University of Life Sciences)H-Index: 12
Last.Priit Väljamäe (UT: University of Tartu)H-Index: 19
view all 7 authors...
23 CitationsSource
#1Silja Kuusk (UT: University of Tartu)H-Index: 8
#2Priit Väljamäe (UT: University of Tartu)H-Index: 19
Background β-glucosidases (BGs) catalyze the hydrolysis of β-glycosidic bonds in glucose derivatives. They constitute an important group of enzymes with biotechnological interest like supporting cellulases in degradation of lignocellulose to fermentable sugars. In the latter context, the glucose tolerant BGs are of particular interest. These BGs often show peculiar kinetics, including inhibitory effects of substrates and activating effects of inhibitors, such as glucose or xylose. The mechanisms...
16 CitationsSource
#1Silja Kuusk (UT: University of Tartu)H-Index: 8
#2Morten Sørlie (NMBU: Norwegian University of Life Sciences)H-Index: 30
Last.Priit Väljamäe (UT: University of Tartu)H-Index: 19
view all 3 authors...
Human chitotriosidase (HCHT) is involved in immune response to chitin-containing pathogens in humans. The enzyme is able to degrade chitooligosaccharides as well as crystalline chitin. The catalytic domain of HCHT is connected to the carbohydrate binding module (CBM) through a flexible hinge region. In humans, two active isoforms of HCHT are found–the full length enzyme and its truncated version lacking CBM and the hinge region. The active site architecture of HCHT is reminiscent to that of the ...
3 CitationsSource
#1Mihhail KurašinH-Index: 5
#2Silja KuuskH-Index: 8
Last.Priit VäljamäeH-Index: 19
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Abstract Processive glycoside hydrolases are the key components of enzymatic machineries that decompose recalcitrant polysaccharides, such as chitin and cellulose. The intrinsic processivity (PIntr) of cellulases has been shown to be governed by the rate constant of dissociation from polymer chain (koff). However, the reported koff values of cellulases are strongly dependent on the method used for their measurement. Here, we developed a new method for determining koff, based on measuring the exc...
15 CitationsSource
#1Silja Kuusk (UT: University of Tartu)H-Index: 8
#2Morten Sørlie (NMBU: Norwegian University of Life Sciences)H-Index: 30
Last.Priit Väljamäe (UT: University of Tartu)H-Index: 19
view all 3 authors...
Abstract Processive enzymes are major components of the efficient enzyme systems that are responsible for the degradation of the recalcitrant polysaccharides cellulose and chitin. Despite intensive research, there is no consensus on which step is rate limiting for these enzymes. Here, we performed a comparative study of two well-characterized enzymes, the cellobiohydrolase Cel7A from Hypocrea jecorina and the chitinase ChiA from Serratia marcescens. Both enzymes were inhibited by their disacchar...
28 CitationsSource
#1Priit Jõers (UT: University of Tartu)H-Index: 9
#2Joachim M. Gerhold (UT: University of Tartu)H-Index: 9
Last.Juhan Sedman (UT: University of Tartu)H-Index: 9
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The mechanistic details of mtDNA maintenance in petite-negative yeasts have remained largely unexplored. We report here that the DNA helicase Hmi1p plays a crucial role in mtDNA stability in Candida albicans . Like its counterpart in Saccharomyces cerevisiae , Hmi1p in C. albicans (CaHmi1p) contains a C-terminal mitochondrial targeting signal that is functional in both organisms. Biochemical analysis demonstrates that CaHmi1p is a protein possessing ATP-dependent 3′–5′ DNA-unwinding activity. De...
9 CitationsSource
#1Silja KuuskH-Index: 8
#2Tiina SedmanH-Index: 8
Last.Juhan SedmanH-Index: 6
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Abstract Hmi1p is a Saccharomyces cerevisiae mitochondrial DNA helicase that is essential for the maintenance of functional mitochondrial DNA. Hmi1p belongs to the superfamily 1 of helicases and is a close homologue of bacterial PcrA and Rep helicases. We have overexpressed and purified recombinant Hmi1p from Escherichia coli and describe here the biochemical characteristics of its DNA helicase activities. Among nucleotide cofactors, the DNA unwinding by Hmi1p was found to occur efficiently only...
23 CitationsSource
#1Tiina Sedman (UT: University of Tartu)H-Index: 8
#2Priit Jõers (UT: University of Tartu)H-Index: 9
Last.Juhan Sedman (UT: University of Tartu)H-Index: 9
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Hmi1p is a helicase in the yeast Saccharomyces cerevisiae required for maintenance of the wild-type mitochondrial genome. Disruption of the HMI1 ORF generates ρ− and ρ0 cells. Here we demonstrate that, in ρ− yeast strains, Hmi1p stimulates the synthesis of long concatemeric mitochondrial DNA molecules associated with a reduction in the number of nucleoids used for mitochondrial DNA packaging. Surprisingly, the ATPase negative mutants of Hmi1p can also stimulate the synthesis of long concatemeric...
22 CitationsSource
#1Tiina Sedman (UT: University of Tartu)H-Index: 8
#2Silja Kuusk (UT: University of Tartu)H-Index: 8
Last.Juhan Sedman (UT: University of Tartu)H-Index: 9
view all 4 authors...
A novel DNA helicase, a homolog of several prokaryotic helicases, including Escherichia coli Rep and UvrD proteins, is encoded by the Saccharomyces cerevisiae nuclear genome open reading frame YOL095c on the chromosome XV. Our data demonstrate that the helicase is localized in the yeast mitochondria and is loosely associated with the mitochondrial inner membrane during biochemical fractionation. The sequence of the C-terminal end of the 80-kDa helicase protein is similar to a typical N-terminal ...
47 CitationsSource
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