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Characterization of monomeric DNA-binding protein Histone H1 in Leishmania braziliensis

Published online by Cambridge University Press:  18 July 2011

EMMA CARMELO ,
GLORIA GONZÁLEZ ,
TERESA CRUZ ,
ANTONIO OSUNA ,
MARIANO HERNÁNDEZ  and
BASILIO VALLADARES
EMMA CARMELO*
Affiliation:
Instituto de Enfermedades Tropicales y Salud Pública de Canarias. Universidad de La Laguna. Av. Astrofisico Fco. Sanchez, s/n. 38202 La Laguna, Tenerife, Spain
GLORIA GONZÁLEZ
Affiliation:
Instituto de Biotecnología, Universidad de Granada. Campus Fuentenueva 18071, Granada, Spain
TERESA CRUZ
Affiliation:
Instituto de Biotecnología, Universidad de Granada. Campus Fuentenueva 18071, Granada, Spain
ANTONIO OSUNA
Affiliation:
Instituto de Biotecnología, Universidad de Granada. Campus Fuentenueva 18071, Granada, Spain
MARIANO HERNÁNDEZ
Affiliation:
Instituto de Enfermedades Tropicales y Salud Pública de Canarias. Universidad de La Laguna. Av. Astrofisico Fco. Sanchez, s/n. 38202 La Laguna, Tenerife, Spain
BASILIO VALLADARES
Affiliation:
Instituto de Enfermedades Tropicales y Salud Pública de Canarias. Universidad de La Laguna. Av. Astrofisico Fco. Sanchez, s/n. 38202 La Laguna, Tenerife, Spain
*
*Corresponding author: Instituto de Enfermedades Tropicales y Salud Pública de Canarias. Universidad de La Laguna. Av. Astrofisico Fco. Sanchez, s/n. 38202 La Laguna, Tenerife, Spain. Tel: 0034 922316502 ext. 6109. Fax: 0034 922318514. E-mail: [email protected]
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Summary

Histone H1 in Leishmania presents relevant differences compared to higher eukaryote counterparts, such as the lack of a DNA-binding central globular domain. Despite that, it is apparently fully functional since its differential expression levels have been related to changes in chromatin condensation and infectivity, among other features. The localization and the aggregation state of L. braziliensis H1 has been determined by immunolocalization, mass spectrometry, cross-linking and electrophoretic mobility shift assays. Analysis of H1 sequences from the Leishmania Genome Database revealed that our protein is included in a very divergent group of histones H1 that is present only in L. braziliensis. An antibody raised against recombinant L. braziliensis H1 recognized specifically that protein by immunoblot in L. braziliensis extracts, but not in other Leishmania species, a consequence of the sequence divergences observed among Leishmania species. Mass spectrometry analysis and in vitro DNA-binding experiments have also proven that L. braziliensis H1 is monomeric in solution, but oligomerizes upon binding to DNA. Finally, despite the lack of a globular domain, L. braziliensis H1 is able to form complexes with DNA in vitro, with higher affinity for supercoiled compared to linear DNA.

Keywords

Leishmania braziliensisHistone H1DNA-binding proteins
Type
Research Article
Information
Parasitology , Volume 138 , Issue 9 , August 2011 , pp. 1093 - 1101
Copyright
Copyright © Cambridge University Press 2011

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