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

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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
Original languageEnglish
JournalMolecular Microbiology
Volume20
Issue number2
Pages (from-to)295-311
Number of pages16
ISSN0950-382X
Publication statusPublished - 1996

Bibliographical 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

ID: 2982615