原创力文档a unique modification of the eukaryotic initiation factor 5a shows the presence of the complete hypusine pathway in leishmania donovani真核生物的一个独特的修改起始因子5显示了杜氏利什曼虫中的完整hypusine通路的存在.pdfVIP
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a unique modification of the eukaryotic initiation factor 5a shows the presence of the complete hypusine pathway in leishmania donovani真核生物的一个独特的修改起始因子5显示了杜氏利什曼虫中的完整hypusine通路的存在
A Unique Modification of the Eukaryotic Initiation Factor
5A Shows the Presence of the Complete Hypusine
Pathway in Leishmania donovani
1 1 2 1 2
Bhavna Chawla , Ravi Ranjan Kumar , Nidhi Tyagi , Gowri Subramanian , N. Srinivasan , Myung Hee
3 1
Park , Rentala Madhubala *
1 School of Life Sciences, Jawaharlal Nehru University, New Delhi, India, 2 Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India, 3 Oral and Pharyngeal
Cancer Branch, National Institute of Dental and Craniofacial Research (NIDCR), National Institute of Health, Bethesda, Maryland, United States of America
Abstract
Deoxyhypusine hydroxylase (DOHH) catalyzes the final step in the post-translational synthesis of an unusual amino acid
hypusine (NJ-(4-amino-2-hydroxybutyl) lysine), which is present on only one cellular protein, eukaryotic initiation factor 5A
(eIF5A). We present here the molecular and structural basis of the function of DOHH from the protozoan parasite,
Leishmania donovani, which causes visceral leishmaniasis. The L. donovani DOHH gene is 981 bp and encodes a putative
polypeptide of 326 amino acids. DOHH is a HEAT-repeat protein with eight tandem repeats of a-helical pairs. Four
conserved histidine-glutamate sequences have been identified that may act as metal coordination sites. A ,42 kDa
recombinant protein with a His-tag was obtained by heterologous expression of DOHH in Escherichia coli. Purified
recombinant DOHH effectively catalyzed the hydroxylation of the intermediate, eIF5A-deoxyhypusine (eIF5A-Dhp), in vit
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