Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/199570
Type: Artigo de periódico
Title: Sir2-related Protein 1 From Leishmania Amazonensis Is A Glycosylated Nad+-dependent Deacetylase.
Author: Fessel, M R
Lira, C B
Giorgio, S
Ramos, C H I
Cano, M I N
Abstract: Sirtuin proteins form a family of NAD+-dependent protein deacetylases that are considered potential drug targets against parasites. Here, we present the first characterization of a sirtuin orthologue from Leishmania amazonensis, an aetiological agent of American tegumentary leishmaniasis that has been the subject of many studies focused in the development of therapeutic approaches. The protein has high sequence identity with other Kinetoplastid Silent information regulator 2 Related Protein 1 (Sir2RP1) and was named LaSir2RP1. The gene exists as a single copy, encoding a monomeric protein (LaSir2RP1) of approximately 41 kDa that has NAD+-dependent deacetylase activity. LaSir2RP1 was immunodetected in total protein extracts, in cytoplasmic granules, and in the secreted material of both promastigotes and lesion-derived amastigotes. Analysis of both lectin‑affinity purified promastigote and amastigote extracts revealed the presence of a major enriched protein of approximately 66 kDa that was recognized by an anti-LaSir2RP1 serum, suggesting that a parasite sirtuin could be glycosylated in vivo.
Subject: Amino Acid Sequence
Animals
Blotting, Western
Circular Dichroism
Cloning, Molecular
Cytoplasmic Granules
Escherichia Coli
Gene Dosage
Glycosylation
Humans
Immunochemistry
Leishmania Mexicana
Leishmaniasis, Cutaneous
Mice
Mice, Inbred Balb C
Molecular Sequence Data
Molecular Weight
Nad
Plasmids
Polymerase Chain Reaction
Protozoan Proteins
Recombinant Proteins
Sequence Alignment
Sirtuins
Rights: fechado
Identifier DOI: 10.1017/S0031182011001077
Address: http://www.ncbi.nlm.nih.gov/pubmed/21819639
Date Issue: 2011
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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