The 18-kilodalton Chlamydia trachomatis histone H1-like protein (Hc1) contains a potential N-terminal dimerization site and a C-terminal nucleic acid-binding domain.

Lotte Bang Pedersen; S Birkelund; A Holm; S Ostergaard; G Christiansen

The 18-kilodalton Chlamydia trachomatis histone H1-like protein (Hc1) contains a potential N-terminal dimerization site and a C-terminal nucleic acid-binding domain.

Lotte Bang Pedersen, S Birkelund, A Holm, S Ostergaard, G Christiansen

Cellebiologi og Fysiologi

6 Citationer (Scopus)

Abstract

The Chlamydia trachomatis histone H1-like protein (Hc1) is a DNA-binding protein specific for the metabolically inactive chlamydial developmental form, the elementary body. Hc1 induces DNA condensation in Escherichia coli and is a strong inhibitor of transcription and translation. These effects may, in part, be due to Hc1-mediated alterations of DNA topology. To locate putative functional domains within Hc1, polypeptides Hc1(2-57) and Hc1(53-125), corresponding to the N- and C-terminal parts of Hc1, respectively, were generated. By chemical cross-linking with ethylene glycol-bis (succinic acid N-hydroxysuccinimide ester), purified recombinant Hc1 was found to form dimers. The dimerization site was located in the N-terminal part of Hc1 (Hc1(2-57)). Moreover, circular dichroism measurements indicated an overall alpha-helical structure of this region. By using limited proteolysis, Southwestern blotting, and gel retardation assays, Hc1(53-125) was shown to contain a domain capable of binding both DNA and RNA. Under the same conditions, Hc1(2-57) had no nucleic acid-binding activity. Electron microscopy of Hc1-DNA and Hc1(53-125)-DNA complexes revealed differences suggesting that the N-terminal part of Hc1 may affect the DNA-binding properties of Hc1.
Udgivelsesdato: 1996-Feb

Originalsprog	Engelsk
Tidsskrift	Journal of Bacteriology
Vol/bind	178
Udgave nummer	4
Sider (fra-til)	994-1002
Antal sider	8
ISSN	0021-9193
Status	Udgivet - 1996

Citationsformater

@article{edf5db90e91511dcbee902004c4f4f50,

title = "The 18-kilodalton Chlamydia trachomatis histone H1-like protein (Hc1) contains a potential N-terminal dimerization site and a C-terminal nucleic acid-binding domain.",

abstract = "The Chlamydia trachomatis histone H1-like protein (Hc1) is a DNA-binding protein specific for the metabolically inactive chlamydial developmental form, the elementary body. Hc1 induces DNA condensation in Escherichia coli and is a strong inhibitor of transcription and translation. These effects may, in part, be due to Hc1-mediated alterations of DNA topology. To locate putative functional domains within Hc1, polypeptides Hc1(2-57) and Hc1(53-125), corresponding to the N- and C-terminal parts of Hc1, respectively, were generated. By chemical cross-linking with ethylene glycol-bis (succinic acid N-hydroxysuccinimide ester), purified recombinant Hc1 was found to form dimers. The dimerization site was located in the N-terminal part of Hc1 (Hc1(2-57)). Moreover, circular dichroism measurements indicated an overall alpha-helical structure of this region. By using limited proteolysis, Southwestern blotting, and gel retardation assays, Hc1(53-125) was shown to contain a domain capable of binding both DNA and RNA. Under the same conditions, Hc1(2-57) had no nucleic acid-binding activity. Electron microscopy of Hc1-DNA and Hc1(53-125)-DNA complexes revealed differences suggesting that the N-terminal part of Hc1 may affect the DNA-binding properties of Hc1. Udgivelsesdato: 1996-Feb",

author = "Pedersen, {Lotte Bang} and S Birkelund and A Holm and S Ostergaard and G Christiansen",

note = "Keywords: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Chlamydia trachomatis; Circular Dichroism; Cloning, Molecular; Cross-Linking Reagents; DNA; DNA-Binding Proteins; Histones; Immunoblotting; Models, Molecular; Molecular Sequence Data; Peptide Fragments; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protozoan Proteins; RNA; RNA-Binding Proteins; Recombinant Proteins; Sequence Analysis; Structure-Activity Relationship",

year = "1996",

language = "English",

volume = "178",

pages = "994--1002",

journal = "Journal of Bacteriology",

issn = "0021-9193",

publisher = "American Society for Microbiology",

number = "4",

}

TY - JOUR

T1 - The 18-kilodalton Chlamydia trachomatis histone H1-like protein (Hc1) contains a potential N-terminal dimerization site and a C-terminal nucleic acid-binding domain.

AU - Pedersen, Lotte Bang

AU - Birkelund, S

AU - Holm, A

AU - Ostergaard, S

AU - Christiansen, G

N1 - Keywords: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Chlamydia trachomatis; Circular Dichroism; Cloning, Molecular; Cross-Linking Reagents; DNA; DNA-Binding Proteins; Histones; Immunoblotting; Models, Molecular; Molecular Sequence Data; Peptide Fragments; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protozoan Proteins; RNA; RNA-Binding Proteins; Recombinant Proteins; Sequence Analysis; Structure-Activity Relationship

PY - 1996

Y1 - 1996

N2 - The Chlamydia trachomatis histone H1-like protein (Hc1) is a DNA-binding protein specific for the metabolically inactive chlamydial developmental form, the elementary body. Hc1 induces DNA condensation in Escherichia coli and is a strong inhibitor of transcription and translation. These effects may, in part, be due to Hc1-mediated alterations of DNA topology. To locate putative functional domains within Hc1, polypeptides Hc1(2-57) and Hc1(53-125), corresponding to the N- and C-terminal parts of Hc1, respectively, were generated. By chemical cross-linking with ethylene glycol-bis (succinic acid N-hydroxysuccinimide ester), purified recombinant Hc1 was found to form dimers. The dimerization site was located in the N-terminal part of Hc1 (Hc1(2-57)). Moreover, circular dichroism measurements indicated an overall alpha-helical structure of this region. By using limited proteolysis, Southwestern blotting, and gel retardation assays, Hc1(53-125) was shown to contain a domain capable of binding both DNA and RNA. Under the same conditions, Hc1(2-57) had no nucleic acid-binding activity. Electron microscopy of Hc1-DNA and Hc1(53-125)-DNA complexes revealed differences suggesting that the N-terminal part of Hc1 may affect the DNA-binding properties of Hc1. Udgivelsesdato: 1996-Feb

AB - The Chlamydia trachomatis histone H1-like protein (Hc1) is a DNA-binding protein specific for the metabolically inactive chlamydial developmental form, the elementary body. Hc1 induces DNA condensation in Escherichia coli and is a strong inhibitor of transcription and translation. These effects may, in part, be due to Hc1-mediated alterations of DNA topology. To locate putative functional domains within Hc1, polypeptides Hc1(2-57) and Hc1(53-125), corresponding to the N- and C-terminal parts of Hc1, respectively, were generated. By chemical cross-linking with ethylene glycol-bis (succinic acid N-hydroxysuccinimide ester), purified recombinant Hc1 was found to form dimers. The dimerization site was located in the N-terminal part of Hc1 (Hc1(2-57)). Moreover, circular dichroism measurements indicated an overall alpha-helical structure of this region. By using limited proteolysis, Southwestern blotting, and gel retardation assays, Hc1(53-125) was shown to contain a domain capable of binding both DNA and RNA. Under the same conditions, Hc1(2-57) had no nucleic acid-binding activity. Electron microscopy of Hc1-DNA and Hc1(53-125)-DNA complexes revealed differences suggesting that the N-terminal part of Hc1 may affect the DNA-binding properties of Hc1. Udgivelsesdato: 1996-Feb

M3 - Journal article

C2 - 8576073

SN - 0021-9193

VL - 178

SP - 994

EP - 1002

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 4

ER -