INGEBI   02650
INSTITUTO DE INVESTIGACIONES EN INGENIERIA GENETICA Y BIOLOGIA MOLECULAR "DR. HECTOR N TORRES"
Unidad Ejecutora - UE
artículos
Título:
The VIPER elements of trypanosomes constitute a novel group tyrosine recombinase-encoding retrotransposons
Autor/es:
LORENZI, H., ROBLEDO, G., LEVIN, M.J.
Revista:
Molecular & Biochemical Parasitology
Editorial:
Elsevier
Referencias:
Año: 2006 vol. 145 p. 184 - 194
Resumen:
Abstract
VIPER was initially characterized as a 2326 bp LTR-like retroelement associated to SIRE, a short interspersed repetitive element specific of
Trypanosoma cruzi. It carried a single ORF that coded for a putative reverse transcriptase-RNAse H protein, suggesting that it could be a truncated
copy of a longer retroelement. Herein we report the identification and characterization of a complete 4480 bp long VIPER in the T. cruzi genome.
The complete VIPER harbored three non-overlapped domains encoding for a GAG-like, a tyrosine recombinase and a reverse transcriptase-RNAse
H proteins. VIPER elements were also found in the genomes of Trypanosoma brucei and Trypanosoma vivax, but not in Leishmania sp. On
the basis of its reverse transcriptase phylogeny, VIPER was classified as an LTR retroelement. However, VIPER was structurally related to the
tyrosine recombinase encoding retroelements, DIRS and Ngaro. Phylogenetic analysis showed that VIPERs tyrosine recombinase grouped with
the transposases RCI1 of Escherichia coli and Ye24 and Ye72 of Haemophilus in.uenzae within a major branch of prokaryotic recombinases.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
the basis of its reverse transcriptase phylogeny, VIPER was classified as an LTR retroelement. However, VIPER was structurally related to the
tyrosine recombinase encoding retroelements, DIRS and Ngaro. Phylogenetic analysis showed that VIPERs tyrosine recombinase grouped with
the transposases RCI1 of Escherichia coli and Ye24 and Ye72 of Haemophilus in.uenzae within a major branch of prokaryotic recombinases.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
The complete VIPER harbored three non-overlapped domains encoding for a GAG-like, a tyrosine recombinase and a reverse transcriptase-RNAse
H proteins. VIPER elements were also found in the genomes of Trypanosoma brucei and Trypanosoma vivax, but not in Leishmania sp. On
the basis of its reverse transcriptase phylogeny, VIPER was classified as an LTR retroelement. However, VIPER was structurally related to the
tyrosine recombinase encoding retroelements, DIRS and Ngaro. Phylogenetic analysis showed that VIPERs tyrosine recombinase grouped with
the transposases RCI1 of Escherichia coli and Ye24 and Ye72 of Haemophilus in.uenzae within a major branch of prokaryotic recombinases.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
the basis of its reverse transcriptase phylogeny, VIPER was classified as an LTR retroelement. However, VIPER was structurally related to the
tyrosine recombinase encoding retroelements, DIRS and Ngaro. Phylogenetic analysis showed that VIPERs tyrosine recombinase grouped with
the transposases RCI1 of Escherichia coli and Ye24 and Ye72 of Haemophilus in.uenzae within a major branch of prokaryotic recombinases.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
copy of a longer retroelement. Herein we report the identification and characterization of a complete 4480 bp long VIPER in the T. cruzi genome.
The complete VIPER harbored three non-overlapped domains encoding for a GAG-like, a tyrosine recombinase and a reverse transcriptase-RNAse
H proteins. VIPER elements were also found in the genomes of Trypanosoma brucei and Trypanosoma vivax, but not in Leishmania sp. On
the basis of its reverse transcriptase phylogeny, VIPER was classified as an LTR retroelement. However, VIPER was structurally related to the
tyrosine recombinase encoding retroelements, DIRS and Ngaro. Phylogenetic analysis showed that VIPERs tyrosine recombinase grouped with
the transposases RCI1 of Escherichia coli and Ye24 and Ye72 of Haemophilus in.uenzae within a major branch of prokaryotic recombinases.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
the basis of its reverse transcriptase phylogeny, VIPER was classified as an LTR retroelement. However, VIPER was structurally related to the
tyrosine recombinase encoding retroelements, DIRS and Ngaro. Phylogenetic analysis showed that VIPERs tyrosine recombinase grouped with
the transposases RCI1 of Escherichia coli and Ye24 and Ye72 of Haemophilus in.uenzae within a major branch of prokaryotic recombinases.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
The complete VIPER harbored three non-overlapped domains encoding for a GAG-like, a tyrosine recombinase and a reverse transcriptase-RNAse
H proteins. VIPER elements were also found in the genomes of Trypanosoma brucei and Trypanosoma vivax, but not in Leishmania sp. On
the basis of its reverse transcriptase phylogeny, VIPER was classified as an LTR retroelement. However, VIPER was structurally related to the
tyrosine recombinase encoding retroelements, DIRS and Ngaro. Phylogenetic analysis showed that VIPERs tyrosine recombinase grouped with
the transposases RCI1 of Escherichia coli and Ye24 and Ye72 of Haemophilus in.uenzae within a major branch of prokaryotic recombinases.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
the basis of its reverse transcriptase phylogeny, VIPER was classified as an LTR retroelement. However, VIPER was structurally related to the
tyrosine recombinase encoding retroelements, DIRS and Ngaro. Phylogenetic analysis showed that VIPERs tyrosine recombinase grouped with
the transposases RCI1 of Escherichia coli and Ye24 and Ye72 of Haemophilus in.uenzae within a major branch of prokaryotic recombinases.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.
Taken together, VIPERs structure, the nature of its tyrosine recombinase, the unique features of its reverse transcriptase catalytic consensus motif
and the fact that it was found in Trypanosomes, an early branching eukaryote, suggest that VIPER may be the closest relative of the founder element
of the tyrosine recombinase encoding retrotransposons known up to date. Our analysis revealed that tyrosine recombinase-encoding retroelements
were originated as early in evolution as non-LTR retroelements and suggests that VIPER, Ngaro and DIRS elements may constitute a third group
of retrotransposons, distinct from both LTR and non-LTR retroelements.
© 2005 Elsevier B.V. All rights reserved.