ArticleApplied and environmental microbiology2005
Characterization of a nucleus-encoded chitinase from the yeast Kluyveromyces lactis.
Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 37 citations in OpenAlex.
- Yeast-secreted compounds with antifungal activity-screening, genetic parts, biosynthetic pathways, and regulation.FEMS yeast research · 2025Review
- The N-Acetylglucosamine Kinase fromInternational journal of molecular sciences · 2021Article
- Diversification of Fungal Chitinases and Their Functional Differentiation in Histoplasma capsulatum.Molecular biology and evolution · 2021Article
- Evolutionary Overview of Molecular Interactions and Enzymatic Activities in the Yeast Cell Walls.International journal of molecular sciences · 2020Review
- Complete Genome Sequence ofGenome announcements · 2017Article
- Fungal chitinases: function, regulation, and potential roles in plant/pathogen interactions.Current genetics · 2016Review
- Chitinases Are Essential for Cell Separation in Ustilago maydis.Eukaryotic cell · 2015Article
- Functional characterization of extracellular chitinase encoded by the YlCTS1 gene in a dimorphic yeast Yarrowia lipolytica.Journal of microbiology (Seoul, Korea) · 2014Article
- Expression of heparan sulfate sulfotransferases in Kluyveromyces lactis and preparation of 3'-phosphoadenosine-5'-phosphosulfate.Glycobiology · 2011Article
- CelAB, a multifunctional cellulase encoded by Teredinibacter turnerae T7902T, a culturable symbiont isolated from the wood-boring marine bivalve Lyrodus pedicellatus.Applied and environmental microbiology · 2007Article
- Review of fungal chitinases.Mycopathologia · 2006Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endogenous proteins secreted from Kluyveromyces lactis were screened for their ability to bind to or to hydrolyze chitin. This analysis resulted in identification of a nucleus-encoded extracellular chitinase (KlCts1p) with a chitinolytic activity distinct from that of the plasmid-encoded killer toxin alpha-subunit. Sequence analysis of cloned KlCTS1 indicated that it encodes a 551-amino-acid chitinase having a secretion signal peptide, an amino-terminal family 18 chitinase catalytic domain, a serine-threonine-rich domain, and a carboxy-terminal type 2 chitin-binding domain. The association of purified KlCts1p with chitin is stable in the presence of high salt concentrations and pH 3 to 10 buffers; however, complete dissociation and release of fully active KlCts1p occur in 20 mM NaOH. Similarly, secreted human serum albumin harboring a carboxy-terminal fusion with the chitin-binding domain derived from KlCts1p also dissociates from chitin in 20 mM NaOH, demonstrating the domain's potential utility as an affinity tag for reversible chitin immobilization or purification of alkaliphilic or alkali-tolerant recombinant fusion proteins. Finally, haploid K. lactis cells harboring a cts1 null mutation are viable but exhibit a cell separation defect, suggesting that KlCts1p is required for normal cytokinesis, probably by facilitating the degradation of septum-localized chitin.
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Registered trials
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