The recombinant product of the Chryptomonas phi plastid gene hlpA is an architectural HU-like protein that promotes the assembly of complex nucleoprotein structures

Détails

ID Serval
serval:BIB_F99E0FA6AFCA
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The recombinant product of the Chryptomonas phi plastid gene hlpA is an architectural HU-like protein that promotes the assembly of complex nucleoprotein structures
Périodique
European Journal of Biochemistry
Auteur(s)
Grasser  K. D., Ritt  C., Krieg  M., Fernandez  S., Alonso  J. C., Grimm  R.
ISSN
0014-2956 (Print)
Statut éditorial
Publié
Date de publication
10/1997
Volume
249
Numéro
1
Pages
70-6
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Oct 1
Résumé
The HlpA protein which is encoded by the hlpA gene in the plastid genome of the cryptomonad alga Chryptomonas phi is structurally related to the non-sequence-specific DNA-binding and DNA-bending HU family of chromatin-associated proteins. The expression of the HlpA protein complements the mutant phenotype of Bacillus subtilis cells impaired in the Hbsu protein (B. subtilis HU), as measured by the resistance of the cells to methylmethane sulphonate. To analyse the interactions of HlpA with DNA, we expressed the protein in Escherichia coli and purified it to homogeneity. HlpA interacts preferentially with four-way junction DNA or DNA minicircles, when compared with linear DNA, recognising DNA structure. HlpA and E. coli HU display comparable affinities for all types of DNA tested; however, HlpA exhibits a stronger tendency to self-associate in the presence of DNA. Accordingly, HlpA oligomerises more readily than HU in protein crosslinking experiments. In the presence of topoisomerase I, HlpA constrains negative superhelical turns in closed circular plasmid DNA. The HlpA protein mediates the joining of distant recombination sites into a complex nucleoprotein structure, as judged by beta-mediated site-specific recombination. The results presented provide evidence that HlpA is a functional plastid equivalent of nuclear and mitochondrial HMG1-like proteins and bacterial HU proteins.
Mots-clé
Algae/chemistry/genetics/*metabolism Bacillus subtilis/genetics Bacterial Proteins/chemistry/genetics/metabolism Base Sequence DNA/chemistry/metabolism DNA Primers/genetics DNA-Binding Proteins/*chemistry/genetics/*metabolism Dimerization Escherichia coli/genetics Genetic Complementation Test Nucleoproteins/chemistry/genetics/metabolism Plant Proteins/*chemistry/genetics/*metabolism Plastids/genetics Polymerase Chain Reaction Protein Binding Recombinant Proteins/chemistry/genetics/metabolism
Pubmed
Web of science
Création de la notice
25/01/2008 14:52
Dernière modification de la notice
20/08/2019 17:25
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