Purification of recombinant Chlamydia trachomatis histone H1-like protein Hc2, and comparative functional analysis of Hc2 and Hc1.

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Standard

Purification of recombinant Chlamydia trachomatis histone H1-like protein Hc2, and comparative functional analysis of Hc2 and Hc1. / Pedersen, Lotte Bang; Birkelund, S; Christiansen, G.

I: Molecular Microbiology, Bind 20, Nr. 2, 1996, s. 295-311.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Pedersen, LB, Birkelund, S & Christiansen, G 1996, 'Purification of recombinant Chlamydia trachomatis histone H1-like protein Hc2, and comparative functional analysis of Hc2 and Hc1.', Molecular Microbiology, bind 20, nr. 2, s. 295-311.

APA

Pedersen, L. B., Birkelund, S., & Christiansen, G. (1996). Purification of recombinant Chlamydia trachomatis histone H1-like protein Hc2, and comparative functional analysis of Hc2 and Hc1. Molecular Microbiology, 20(2), 295-311.

Vancouver

Pedersen LB, Birkelund S, Christiansen G. Purification of recombinant Chlamydia trachomatis histone H1-like protein Hc2, and comparative functional analysis of Hc2 and Hc1. Molecular Microbiology. 1996;20(2):295-311.

Author

Pedersen, Lotte Bang ; Birkelund, S ; Christiansen, G. / Purification of recombinant Chlamydia trachomatis histone H1-like protein Hc2, and comparative functional analysis of Hc2 and Hc1. I: Molecular Microbiology. 1996 ; Bind 20, Nr. 2. s. 295-311.

Bibtex

@article{0f61eb20e91611dcbee902004c4f4f50,
title = "Purification of recombinant Chlamydia trachomatis histone H1-like protein Hc2, and comparative functional analysis of Hc2 and Hc1.",
abstract = "The metabolically inactive developmental form of Chlamydia trachomatis, the elementary body, contains two very basic DNA-binding proteins with homology to eukaryotic histone H1. One of these, Hc1, is relatively well characterized and induces DNA condensation in vitro, whereas the other, Hc2, is functionally virtually uncharacterized. In this study we describe the purification of Hc2, and a detailed comparative functional analysis of Hc2 and Hc1 is presented. By gel shift assays and electron microscopy, marked differences in the nucleic acid-binding properties of Hc2 and Hc1 were observed. Furthermore, Hc2 was found to strongly inhibit translation and transcription in vitro. Our results imply that DNA condensation is not the only function of Hc2. Udgivelsesdato: 1996-Apr",
author = "Pedersen, {Lotte Bang} and S Birkelund and G Christiansen",
note = "Keywords: Antibodies, Bacterial; Bacterial Proteins; Base Sequence; Chlamydia trachomatis; DNA, Bacterial; DNA-Binding Proteins; Endopeptidases; Escherichia coli; Factor Xa; Histones; Molecular Sequence Data; Protein Biosynthesis; Protozoan Proteins; RNA, Viral; RNA-Binding Proteins; Recombinant Fusion Proteins; Repressor Proteins; Transcription, Genetic",
year = "1996",
language = "English",
volume = "20",
pages = "295--311",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley-Blackwell",
number = "2",

}

RIS

TY - JOUR

T1 - Purification of recombinant Chlamydia trachomatis histone H1-like protein Hc2, and comparative functional analysis of Hc2 and Hc1.

AU - Pedersen, Lotte Bang

AU - Birkelund, S

AU - Christiansen, G

N1 - Keywords: Antibodies, Bacterial; Bacterial Proteins; Base Sequence; Chlamydia trachomatis; DNA, Bacterial; DNA-Binding Proteins; Endopeptidases; Escherichia coli; Factor Xa; Histones; Molecular Sequence Data; Protein Biosynthesis; Protozoan Proteins; RNA, Viral; RNA-Binding Proteins; Recombinant Fusion Proteins; Repressor Proteins; Transcription, Genetic

PY - 1996

Y1 - 1996

N2 - The metabolically inactive developmental form of Chlamydia trachomatis, the elementary body, contains two very basic DNA-binding proteins with homology to eukaryotic histone H1. One of these, Hc1, is relatively well characterized and induces DNA condensation in vitro, whereas the other, Hc2, is functionally virtually uncharacterized. In this study we describe the purification of Hc2, and a detailed comparative functional analysis of Hc2 and Hc1 is presented. By gel shift assays and electron microscopy, marked differences in the nucleic acid-binding properties of Hc2 and Hc1 were observed. Furthermore, Hc2 was found to strongly inhibit translation and transcription in vitro. Our results imply that DNA condensation is not the only function of Hc2. Udgivelsesdato: 1996-Apr

AB - The metabolically inactive developmental form of Chlamydia trachomatis, the elementary body, contains two very basic DNA-binding proteins with homology to eukaryotic histone H1. One of these, Hc1, is relatively well characterized and induces DNA condensation in vitro, whereas the other, Hc2, is functionally virtually uncharacterized. In this study we describe the purification of Hc2, and a detailed comparative functional analysis of Hc2 and Hc1 is presented. By gel shift assays and electron microscopy, marked differences in the nucleic acid-binding properties of Hc2 and Hc1 were observed. Furthermore, Hc2 was found to strongly inhibit translation and transcription in vitro. Our results imply that DNA condensation is not the only function of Hc2. Udgivelsesdato: 1996-Apr

M3 - Journal article

C2 - 8733229

VL - 20

SP - 295

EP - 311

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 2

ER -

ID: 2982615