Katarzyna Kuczek

Polish Academy of Sciences

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M Mordarski

Polish Academy of Sciences

Magdalena Kotowska

Ludwik Hirszfeld Institute of Immunology and Experimental Therapy

Krzysztof Pawlik

Polish Academy of Sciences

Eriko Takano

University of Manchester

Eric Cundliffe

University of Leicester

Andrew R. Butler

International Centre for Radio Astronomy Research

Aleksandra Smulczyk-Krawczyszyn

Ludwik Hirszfeld Institute of Immunology and Experimental Therapy

Anna Gaszewska-Mastalarz

Augusta University

Jolanta Zakrzewska‐Czerwińska

University of Wrocław

Michael Goodfellow

Newcastle University

Cooperative Institutions

Ludwik Hirszfeld Institute of Immunology and Experimental Therapy

Polish Academy of Sciences

Norwich Research Park

University of Wrocław

Newcastle University

John Innes Centre

Institute of Immunology

Max Planck Institute for Molecular Genetics

Polish Academy of Learning

University of Cologne

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DNA restriction endonuclease analysis of some Streptomyces species.

PubMed (1991)

Jolanta Zakrzewska‐Czerwińska Katarzyna Kuczek Anna Gaszewska-Mastalarz M Mordarski

Streptomycetaceae

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Citations (3)

Distribution of oxoacyl synthase homology sequences within Streptomyces DNA

FEMS Microbiology Letters (1994)

Katarzyna Kuczek

A genomic DNA sequence of Streptomyces strain ISP 5485 was cloned, sequenced and compared with corresponding information from nucleic acid data banks. The DNA sequence was unique, but showed homology to DNA coding for the condensing enzyme, 2-oxoacyl synthase, of the deoxyerythronolide B synthase complex (DEBS) from Saccharopolyspora erythraea NRRL 2338. A subfragment of the sequenced DNA was used to construct a gene-specific probe that formed part of the putative 2-oxoacyl synthase gene. The PCR-amplified and labelled probe was used in hybridization experiments involving 33 streptomycete strains that produced different classes of antibiotics. The probe showed widespread homology with DNA considered to be part of analogous genes within genomes of different polyketide producers. The implications of the probe homology to bacterial chromosomal DNA are discussed.

Homology

Polyketide synthase

genomic DNA

Streptomycetaceae

10.1016/0378-1097(94)90523-1

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Bacterial colony screening with aStreptomycesDNA probe

FEMS Microbiology Letters (1989)

Katarzyna Kuczek M Mordarski

Restriction fragments of 1.5 kb–3.5 kb length were selected from a SalI digest of Streptomyces coriofaciens ISP5485 DNA. After radiolabelling, these fragments were used as a molecular probe. A number of actinomycetes was screened in colony hybridization. Streptomyces and Streptoverticillium strains were recognized by the probe and the hybridization sensitivity was high with isolated DNA.

Streptomycetaceae

Hybridization probe

Molecular probe

DNA–DNA hybridization

10.1111/j.1574-6968.1989.tb03633.x

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Citations (4)

Streptomyces coelicolor DNA homologous with acyltransferase domains of type I polyketide synthase gene complex

FEMS Microbiology Letters (2006)

Katarzyna Kuczek Krzysztof Pawlik Magdalena Kotowska M Mordarski

An acyltransferase-homologous DNA fragment was amplified in a PCR reaction on a cosmid DNA template from the genomic DNA library of the soil bacterium Streptomyces coelicolor A3(2). The putative amino acid sequence of the fragment resembles acyl-CoA:ACP acyltransferase domains from several bacterial enzymatic complexes of polyketide synthase. There is a high similarity with acyltransferase domains from so-called type I polyketide synthases. Such synthases catalyze production of the aglycone portion of macrolides and polyethers that are important as antibiotics or immunosuppressants. The amplified fragment is considered to be a part of a larger gene complex.

Acyltransferases

Cosmid

Polyketide synthase

Actinorhodin

10.1111/j.1574-6968.1997.tb12773.x

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Citations (11)

[Controlled biosynthesis of polyketide antibiotics].

PubMed (1996)

Katarzyna Kuczek Magdalena Kotowska M Mordarski

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Sequences homological with the beta-ketoacyl synthase gene--their distribution within Streptomyces DNA.

Acta Biochimica Polonica (1994)

Katarzyna Kuczek M Mordarski Michael Goodfellow

Beta-lactam

BETA (programming language)

Streptomycetaceae

10.18388/abp.1994_4736

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Distribution of oxoacyl synthase homology sequences withinStreptomycesDNA

FEMS Microbiology Letters (1994)

Katarzyna Kuczek M Mordarski M. Goodfellow

Homology

Polyketide synthase

genomic DNA

10.1111/j.1574-6968.1994.tb06847.x

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Citations (4)

Streptomyces coelicolor DNA homologous with acyltransferase domains of type I polyketide synthase gene complex

FEMS Microbiology Letters (1997)

Katarzyna Kuczek

Acyltransferases

Cosmid

Polyketide synthase

Actinorhodin

genomic DNA

10.1016/s0378-1097(97)00476-x

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Citations (1)

[Combinatorial biosynthesis of novel macrolides and other complex polyketides].

PubMed (1999)

Katarzyna Kuczek Martyna Kotowska Krzysztof Pawlik

Source

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Type II Thioesterase ScoT, Associated with Streptomyces coelicolor A3(2) Modular Polyketide Synthase Cpk, Hydrolyzes Acyl Residues and Has a Preference for Propionate

Applied and Environmental Microbiology (2008)

Magdalena Kotowska Krzysztof Pawlik Aleksandra Smulczyk-Krawczyszyn Hubert Bartosz-Bechowski Katarzyna Kuczek

Type II thioesterases (TE IIs) were shown to maintain the efficiency of polyketide synthases (PKSs) by removing acyl residues blocking extension modules. However, the substrate specificity and kinetic parameters of these enzymes differ, which may have significant consequences when they are included in engineered hybrid systems for the production of novel compounds. Here we show that thioesterase ScoT associated with polyketide synthase Cpk from Streptomyces coelicolor A3(2) is able to hydrolyze acetyl, propionyl, and butyryl residues, which is consistent with its editing function. This enzyme clearly prefers propionate, in contrast to the TE IIs tested previously, and this indicates that it may have a role in control of the starter unit. We also determined activities of ScoT mutants and concluded that this enzyme is an alpha/beta hydrolase with Ser90 and His224 in its active site.

Thioesterase

Polyketide synthase

Hydrolase

10.1128/aem.01371-08

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Citations (23)