Karol Taylor

Institute of Biochemistry and Biophysics, Polish Academy of Sciences

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Grzegorz Węgrzyn

University of Gdańsk

Alicja Węgrzyn

University of Gdańsk

Grażyna Konopa

University of Gdańsk

Agnieszka Szalewska-Pałasz

University of Gdańsk

Anna Herman-Antosiewicz

Gdańsk Medical University

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Maciej Żylicz

Foundation for Polish Science

Barbara Lipińska

University of Gdańsk

Michał Obuchowski

Gdańsk Medical University

S Srutkowska

University of Gdańsk

Halina Witkiewicz

Proteogenomics Research Institute for Systems Medicine

Cooperative Institutions

University of Gdańsk

Gdańsk Medical University

University of Wisconsin–Madison

Polish Academy of Sciences

Stanford University

Institute of Biochemistry and Biophysics, Polish Academy of Sciences

University of Utah

Washington University in St. Louis

Laboratory of Molecular Genetics

MRC Laboratory of Molecular Biology

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Regulation of Bacteriophage λ Replication

Molecular Microbiology (1998)

Karol Taylor Grzegorz Węgrzyn

Bacteriophage λ is both a model for basic biological studies on the molecular level and a commonly used tool in molecular cloning. In this review we summarise the control of bacteriophage λ development, placing particular attention to the mechanisms involved in the "lysis or lysogeny" decision and the regulation of replication of phage λ DNA, as well as of plasmids derived from this phage.

Lysogenic cycle

Replication

Cloning (programming)

10.1007/978-3-642-72071-0_5

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Citations (23)

Molecular Mechanism of Heat Shock-Provoked Disassembly of the Coliphage λ Replication Complex

Journal of Bacteriology (1998)

Alicja We ̧grzyn Anna Herman-Antosiewicz Karol Taylor Grzegorz We ̧grzyn

We have found previously that, in contrast to the free O initiator protein of lambda phage or plasmid rapidly degraded by the Escherichia coli ClpP/ClpX protease, the lambdaO present in the replication complex (RC) is protected from proteolysis. However, in cells growing in a complete medium, a temperature shift from 30 to 43 degrees C resulted in the decay of the lambdaO fraction, which indicated disassembly of RC. This process occurred due to heat shock induction of the groE operon, coding for molecular chaperones of the Hsp60 system. Here we demonstrate that an increase in the cellular concentration of GroEL and GroES proteins is not in itself sufficient to cause RC disassembly. Another requirement is a DNA gyrase-mediated negative resupercoiling of lambda plasmid DNA, which counteracts DNA relaxation and starts to dominate 10 min after the temperature upshift. We presume that RC dissociates from lambda DNA during the negative resupercoiling, becoming susceptible to the subsequent action of GroELS and ClpP/ClpX proteins. In contrast to lambda cro+, in lambda cro- plasmid-harboring cells, the RC reveals heat shock resistance. After temperature upshift of the lambda crots plasmid-harboring cells, a Cro repressor-independent control of lambda DNA replication and heat shock resistance of RC are established before the period of DNA gyrase-mediated negative supercoiling. We suggest that the tight binding of RC to lambda DNA is due to interaction of RC with other DNA-bound proteins, and is related to the molecular basis of the lambda cro- plasmid replication control.

GroES

Lambda phage

Replicon

10.1128/jb.180.9.2475-2483.1998

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Stability of coliphage λ DNA replication initiator, the λO protein

Journal of Molecular Biology (1992)

Grzegorz Węgrzyn Alicja Pawlowicz Karol Taylor

Coliphage

Proteolysis

10.1016/0022-2836(92)90624-s

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Citations (35)

Protection of Coliphage λO Initiator Protein from Proteolysis in the Assembly of the Replication Complex in Vivo

Virology (1995)

Alicja Węgrzyn Grzegorz Węgrzyn Karol Taylor

Proteolysis

dnaB helicase

Chaperone (clinical)

10.1006/viro.1995.1064

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Citations (36)

THE PRIMOSOME IN φX174 REPLICATION1

Elsevier eBooks (1981)

Peter Burgers Robert L. Low J. Kobori Robert S. Fuller Jon M. Kaguni

10.1016/b978-0-12-583580-0.50032-7

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Citations (1)

Escherichia coli initiator protein DnaA, cell-cycle and control of lambda plasmid replication

Bulletin of the Polish Academy of Sciences. Series Biological Sciences (1996)

Karol Taylor Grzegorz Węgrzyn Alicja Węgrzyn Agnieszka Szalewska-Pałasz Anna Herman-Antosiewicz

DnaA

Lambda phage

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Interactions between Phage λ Replication Proteins, λ DNA and Minicell Membrane

European Journal of Biochemistry (1981)

Maciej Żylicz Karol Taylor

Gentle methods for minicell lysis and lysate fractionation have been elaborated: lysis by T4 lysozyme without detergents, and fractionation by equilibrium sedimentation in a metrizamide density gradient, both at low ionic strength. In the lysates of phage‐λ‐infected minicells the λ DNA, trapped at a prereplicative step [Witkiewicz, H. and Taylor, K. (1979) Biochim. Biophys. Acta 564 , 31–36], appeard in two peaks of different buoyant densities: as a membrane‐bound and a free λ DNA. The covalently‐closed‐circular form of λ DNA appeared exclusively in the membrane fraction. The λ‐coded proteins, synthesized in λ‐infected minicells, appeared in two major fractions: as membrane‐bound and as free proteins, and in one minor fraction, bound with free λ DNA. Neither λ protein engaged in the initiation of DNA replication was present in the fraction of free proteins: the P ‐gene product was membrane‐associated, and the O ‐gene product formed a complex with free λ DNA. The efect of high ionic strength (KCl) and of detergents (Triton X ‐100 and sarcosyl) on the binding of replication proteins with λ DNA and with the membrane was studied. The non‐ionic detergent, Triton X ‐100 caused displacement of a part of λ DNA from the membrane to the free λ DNA peak; both γ replication proteins were bound with free γ DNA. The binding of the O protein with λ DNA was relatively stable, but was destroyed by the ionic detergent, sarcosyl.

10.1111/j.1432-1033.1981.tb05067.x

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Citations (11)

The fate of phage λ DNA in λ-infected minicells

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis (1979)

Halina Witkiewicz Karol Taylor

ColE1

Lambda phage

10.1016/0005-2787(79)90185-0

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Citations (7)

Stringent control of replication of plasmids derived from coliphage λ