Please use this identifier to cite or link to this item: http://sgc.anlis.gov.ar/handle/123456789/1497
Title: Characterization of a Trypanosoma cruzi acetyltransferase: cellular location, activity and structure
Authors: Ochaya, Stephen 
Respuela, Patricia 
Simonsson, Maria 
Saraswathi, Abhiman 
Branche, Carole 
Lee, Jennifer 
Bua, Jacqueline 
Nilsson, Daniel 
Åslund, Lena 
Bontempi, Esteban J 
Andersson, Björn 
Issue Date: Apr-2007
Journal: Molecular and biochemical parasitology 
Abstract: 
Trypanosomatids are widespread parasites that cause three major tropical diseases. In trypanosomatids, as in most other organisms, acetylation is a common protein modification that is important in multiple, diverse processes. This paper describes a new member of the Trypanosoma cruzi acetyltransferase family. The gene is single copy and orthologs are also present in the other two sequenced trypanosomatids, Trypanosoma brucei and Leishmania major. This protein (TcAT-1) has the essential motifs present in members of the GCN5-related acetyltransferase (GNAT) family, as well as an additional motif also found in some enzymes from plant and animal species. The protein is evolutionarily more closely related to this group of enzymes than to histone acetyltransferases. The native protein has a cytosolic cellular location and is present in all three life-cycle stages of the parasite. The recombinant protein was shown to have autoacetylation enzymatic activity.
URI: http://sgc.anlis.gob.ar/handle/123456789/1497
ISSN: 0166-6851
DOI: 10.1016/j.molbiopara.2006.12.009
Appears in Collections:Publicaciones INP

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