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Trypanosoma cruzi MSH2: Functional analyses on different parasite strains provide evidences for a role on the oxidative stress response.

Campos PC, Silva VG, Furtado C, Machado-Silva A, Darocha WD, Peloso EF, Gadelha FR, Medeiros MH, Lana Gde C, Chen Y, Barnes RL, Passos-Silva DG, McCulloch R, Machado CR, Teixeira SM - Mol. Biochem. Parasitol. (2010)

Bottom Line: Here we compared cell survival rates after exposure to genotoxic agents and levels of oxidative stress-induced DNA in different parasite strains.The results suggest that the distinct MSH2 isoforms have differences in their activity.More importantly, they also indicate that, in addition to its role in MMR, TcMSH2 acts in the parasite response to oxidative stress through a novel mitochondrial function that may be conserved in T. brucei.

View Article: PubMed Central - PubMed

Affiliation: Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.

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Sequence analysis of TcMSH2 from CL Brener and Col1.7G2 strains. Alignment between TcMSH2 sequences from Col1.7G2 (T. cruzi I) and sequences corresponding to alleles B and C from CL Brener (T. cruzi II/III hybrid strain). In the N-terminal region, black shading indicates the putative MSH2 mismatch recognition motif, amino acids 89–92. A putative leucine zipper, amino acids 280–300, and a conserved 303 arginine residue are shown by light gray shadings. In the C-terminal region, bolded, underlined amino acids indicate the Walker A motif (P-loop, a Mg2+ binding site), amino acids 709–716, the Q-loop (involved in ATP hydrolysis), amino acids 750–754, the Walker B motif (involved in ATP hydrolysis and within the mutS family signature), amino acids 783–799, and the helix-turn-helix motif, amino acids 869–886. The colored blocks represent the different MutS domains: domains I, II, III, IV and V are indicated by black, gray, pink/cyan, green and red boxes, respectively. Black triangles show amino acid substitutions.
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fig0030: Sequence analysis of TcMSH2 from CL Brener and Col1.7G2 strains. Alignment between TcMSH2 sequences from Col1.7G2 (T. cruzi I) and sequences corresponding to alleles B and C from CL Brener (T. cruzi II/III hybrid strain). In the N-terminal region, black shading indicates the putative MSH2 mismatch recognition motif, amino acids 89–92. A putative leucine zipper, amino acids 280–300, and a conserved 303 arginine residue are shown by light gray shadings. In the C-terminal region, bolded, underlined amino acids indicate the Walker A motif (P-loop, a Mg2+ binding site), amino acids 709–716, the Q-loop (involved in ATP hydrolysis), amino acids 750–754, the Walker B motif (involved in ATP hydrolysis and within the mutS family signature), amino acids 783–799, and the helix-turn-helix motif, amino acids 869–886. The colored blocks represent the different MutS domains: domains I, II, III, IV and V are indicated by black, gray, pink/cyan, green and red boxes, respectively. Black triangles show amino acid substitutions.


Trypanosoma cruzi MSH2: Functional analyses on different parasite strains provide evidences for a role on the oxidative stress response.

Campos PC, Silva VG, Furtado C, Machado-Silva A, Darocha WD, Peloso EF, Gadelha FR, Medeiros MH, Lana Gde C, Chen Y, Barnes RL, Passos-Silva DG, McCulloch R, Machado CR, Teixeira SM - Mol. Biochem. Parasitol. (2010)

Sequence analysis of TcMSH2 from CL Brener and Col1.7G2 strains. Alignment between TcMSH2 sequences from Col1.7G2 (T. cruzi I) and sequences corresponding to alleles B and C from CL Brener (T. cruzi II/III hybrid strain). In the N-terminal region, black shading indicates the putative MSH2 mismatch recognition motif, amino acids 89–92. A putative leucine zipper, amino acids 280–300, and a conserved 303 arginine residue are shown by light gray shadings. In the C-terminal region, bolded, underlined amino acids indicate the Walker A motif (P-loop, a Mg2+ binding site), amino acids 709–716, the Q-loop (involved in ATP hydrolysis), amino acids 750–754, the Walker B motif (involved in ATP hydrolysis and within the mutS family signature), amino acids 783–799, and the helix-turn-helix motif, amino acids 869–886. The colored blocks represent the different MutS domains: domains I, II, III, IV and V are indicated by black, gray, pink/cyan, green and red boxes, respectively. Black triangles show amino acid substitutions.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3142612&req=5

fig0030: Sequence analysis of TcMSH2 from CL Brener and Col1.7G2 strains. Alignment between TcMSH2 sequences from Col1.7G2 (T. cruzi I) and sequences corresponding to alleles B and C from CL Brener (T. cruzi II/III hybrid strain). In the N-terminal region, black shading indicates the putative MSH2 mismatch recognition motif, amino acids 89–92. A putative leucine zipper, amino acids 280–300, and a conserved 303 arginine residue are shown by light gray shadings. In the C-terminal region, bolded, underlined amino acids indicate the Walker A motif (P-loop, a Mg2+ binding site), amino acids 709–716, the Q-loop (involved in ATP hydrolysis), amino acids 750–754, the Walker B motif (involved in ATP hydrolysis and within the mutS family signature), amino acids 783–799, and the helix-turn-helix motif, amino acids 869–886. The colored blocks represent the different MutS domains: domains I, II, III, IV and V are indicated by black, gray, pink/cyan, green and red boxes, respectively. Black triangles show amino acid substitutions.
Bottom Line: Here we compared cell survival rates after exposure to genotoxic agents and levels of oxidative stress-induced DNA in different parasite strains.The results suggest that the distinct MSH2 isoforms have differences in their activity.More importantly, they also indicate that, in addition to its role in MMR, TcMSH2 acts in the parasite response to oxidative stress through a novel mitochondrial function that may be conserved in T. brucei.

View Article: PubMed Central - PubMed

Affiliation: Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.

Show MeSH
Related in: MedlinePlus