Characterization of a Trypanosoma cruzi acetyltransferase:: cellular location, activity and structure

被引:4
作者
Ochaya, Stephen
Respuela, Patricia
Simonsson, Maria
Saraswathi, Abhiman
Branche, Carole
Lee, Jennifer
Bua, Jacqueline
Nilsson, Daniel
Aslund, Lena
Bontempi, Esteban J. [1 ]
Andersson, Bjorn
机构
[1] ANLIS, Inst Nacl Parasitol, RA-1063 Buenos Aires, DF, Argentina
[2] Karolinska Inst, Dept Cell & Mol Biol, Stockholm 17177, Sweden
[3] Rudbeck Lab, Dept Genet & Pathol, S-75185 Uppsala, Sweden
[4] Ludwig Inst Canc Res, S-75124 Uppsala, Sweden
[5] Inst Pasteur, Parasitol Dept, F-75015 Paris, France
[6] Univ Calif Davis, Davis, CA 95616 USA
[7] ANLIS, Inst Nacl Parasitol, RA-1063 Buenos Aires, DF, Argentina
关键词
acetyltransferase; Trypanosoma cruzi; autoacetylation;
D O I
10.1016/j.molbiopara.2006.12.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Trhpanosoma 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. (c) 2006 Elsevier B.V All rights reserved.
引用
收藏
页码:123 / 131
页数:9
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