Identification of novel cyclic nucleotide binding proteins in Trypanosoma cruzi

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Cyclic AMP has been implicated as second messenger in a wide range of cellular processes. In the protozoan parasite Trypanosoma cruzi, cAMP is involved in the development of the parasite's life cycle. While cAMP effectors have been widely studied in other eukaryotic cells, little is known about...

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Autores principales:	Jäger, A.V., De Gaudenzi, J.G., Mild, J.G., Cormack, B.M., Pantano, S., Altschuler, D.L., Edreira, M.M.
Formato:	JOUR
Materias:	cAMP binding proteins cAMP novel effectors cAMP signaling Trypanosoma cruzi cyclic AMP binding protein cyclic AMP dependent protein kinase catalytic subunit proteome protozoal protein carrier protein cyclic nucleotide protein binding amino acid sequence Article computer model controlled study gene segregation molecular model molecular phylogeny nonhuman priority journal protein analysis protein expression protein function protein localization proteomics sequence analysis biology cluster analysis genetics metabolism phylogeny sequence homology Eukaryota Protozoa Carrier Proteins Cluster Analysis Computational Biology Nucleotides, Cyclic Phylogeny Protein Binding Protozoan Proteins Sequence Homology, Amino Acid
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_01666851_v198_n2_p104_Jager
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_01666851_v198_n2_p104_Jager
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spelling	todo:paper_01666851_v198_n2_p104_Jager2023-10-03T15:04:16Z Identification of novel cyclic nucleotide binding proteins in Trypanosoma cruzi Jäger, A.V. De Gaudenzi, J.G. Mild, J.G. Cormack, B.M. Pantano, S. Altschuler, D.L. Edreira, M.M. cAMP binding proteins cAMP novel effectors cAMP signaling Trypanosoma cruzi cyclic AMP binding protein cyclic AMP dependent protein kinase catalytic subunit proteome protozoal protein carrier protein cyclic nucleotide protein binding protozoal protein amino acid sequence Article computer model controlled study gene segregation molecular model molecular phylogeny nonhuman priority journal protein analysis protein expression protein function protein localization proteomics sequence analysis Trypanosoma cruzi biology cluster analysis genetics metabolism phylogeny sequence homology Trypanosoma cruzi Eukaryota Protozoa Trypanosoma cruzi Carrier Proteins Cluster Analysis Computational Biology Nucleotides, Cyclic Phylogeny Protein Binding Protozoan Proteins Sequence Homology, Amino Acid Trypanosoma cruzi Cyclic AMP has been implicated as second messenger in a wide range of cellular processes. In the protozoan parasite Trypanosoma cruzi, cAMP is involved in the development of the parasite's life cycle. While cAMP effectors have been widely studied in other eukaryotic cells, little is known about cAMP's mechanism of action in T. cruzi. To date, only a cAMP-dependent protein kinase A (PKA) has been cloned and characterised in this parasite; however experimental evidence indicates the existence of cAMP-dependent, PKA-independent events. In order to identify new cAMP binding proteins as potential cAMP effectors, we carried out in silico studies using the predicted T. cruzi proteome. Using a combination of search methods 27 proteins with putative cNMP binding domains (CBDs) were identified. Phylogenetic analysis of the CBDs presented a homogeneous distribution, with sequences segregated into two main branches: one containing kinases-like proteins and the other gathering hypothetical proteins with different function or no other known. Comparative modelling of the strongest candidates provides support for the hypothesis that these proteins may give rise to structurally viable cyclic nucleotide binding domains. Pull-down and nucleotide displacement assays strongly suggest that TcCLB.508523.80 could bind cAMP and eventually be a new putative PKA-independent cAMP effector in T. cruzi. © 2015 Elsevier B.V. Fil:Mild, J.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Altschuler, D.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Edreira, M.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_01666851_v198_n2_p104_Jager
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	cAMP binding proteins cAMP novel effectors cAMP signaling Trypanosoma cruzi cyclic AMP binding protein cyclic AMP dependent protein kinase catalytic subunit proteome protozoal protein carrier protein cyclic nucleotide protein binding protozoal protein amino acid sequence Article computer model controlled study gene segregation molecular model molecular phylogeny nonhuman priority journal protein analysis protein expression protein function protein localization proteomics sequence analysis Trypanosoma cruzi biology cluster analysis genetics metabolism phylogeny sequence homology Trypanosoma cruzi Eukaryota Protozoa Trypanosoma cruzi Carrier Proteins Cluster Analysis Computational Biology Nucleotides, Cyclic Phylogeny Protein Binding Protozoan Proteins Sequence Homology, Amino Acid Trypanosoma cruzi
spellingShingle	cAMP binding proteins cAMP novel effectors cAMP signaling Trypanosoma cruzi cyclic AMP binding protein cyclic AMP dependent protein kinase catalytic subunit proteome protozoal protein carrier protein cyclic nucleotide protein binding protozoal protein amino acid sequence Article computer model controlled study gene segregation molecular model molecular phylogeny nonhuman priority journal protein analysis protein expression protein function protein localization proteomics sequence analysis Trypanosoma cruzi biology cluster analysis genetics metabolism phylogeny sequence homology Trypanosoma cruzi Eukaryota Protozoa Trypanosoma cruzi Carrier Proteins Cluster Analysis Computational Biology Nucleotides, Cyclic Phylogeny Protein Binding Protozoan Proteins Sequence Homology, Amino Acid Trypanosoma cruzi Jäger, A.V. De Gaudenzi, J.G. Mild, J.G. Cormack, B.M. Pantano, S. Altschuler, D.L. Edreira, M.M. Identification of novel cyclic nucleotide binding proteins in Trypanosoma cruzi
topic_facet	cAMP binding proteins cAMP novel effectors cAMP signaling Trypanosoma cruzi cyclic AMP binding protein cyclic AMP dependent protein kinase catalytic subunit proteome protozoal protein carrier protein cyclic nucleotide protein binding protozoal protein amino acid sequence Article computer model controlled study gene segregation molecular model molecular phylogeny nonhuman priority journal protein analysis protein expression protein function protein localization proteomics sequence analysis Trypanosoma cruzi biology cluster analysis genetics metabolism phylogeny sequence homology Trypanosoma cruzi Eukaryota Protozoa Trypanosoma cruzi Carrier Proteins Cluster Analysis Computational Biology Nucleotides, Cyclic Phylogeny Protein Binding Protozoan Proteins Sequence Homology, Amino Acid Trypanosoma cruzi
description	Cyclic AMP has been implicated as second messenger in a wide range of cellular processes. In the protozoan parasite Trypanosoma cruzi, cAMP is involved in the development of the parasite's life cycle. While cAMP effectors have been widely studied in other eukaryotic cells, little is known about cAMP's mechanism of action in T. cruzi. To date, only a cAMP-dependent protein kinase A (PKA) has been cloned and characterised in this parasite; however experimental evidence indicates the existence of cAMP-dependent, PKA-independent events. In order to identify new cAMP binding proteins as potential cAMP effectors, we carried out in silico studies using the predicted T. cruzi proteome. Using a combination of search methods 27 proteins with putative cNMP binding domains (CBDs) were identified. Phylogenetic analysis of the CBDs presented a homogeneous distribution, with sequences segregated into two main branches: one containing kinases-like proteins and the other gathering hypothetical proteins with different function or no other known. Comparative modelling of the strongest candidates provides support for the hypothesis that these proteins may give rise to structurally viable cyclic nucleotide binding domains. Pull-down and nucleotide displacement assays strongly suggest that TcCLB.508523.80 could bind cAMP and eventually be a new putative PKA-independent cAMP effector in T. cruzi. © 2015 Elsevier B.V.
format	JOUR
author	Jäger, A.V. De Gaudenzi, J.G. Mild, J.G. Cormack, B.M. Pantano, S. Altschuler, D.L. Edreira, M.M.
author_facet	Jäger, A.V. De Gaudenzi, J.G. Mild, J.G. Cormack, B.M. Pantano, S. Altschuler, D.L. Edreira, M.M.
author_sort	Jäger, A.V.
title	Identification of novel cyclic nucleotide binding proteins in Trypanosoma cruzi
title_short	Identification of novel cyclic nucleotide binding proteins in Trypanosoma cruzi
title_full	Identification of novel cyclic nucleotide binding proteins in Trypanosoma cruzi
title_fullStr	Identification of novel cyclic nucleotide binding proteins in Trypanosoma cruzi
title_full_unstemmed	Identification of novel cyclic nucleotide binding proteins in Trypanosoma cruzi
title_sort	identification of novel cyclic nucleotide binding proteins in trypanosoma cruzi
url	http://hdl.handle.net/20.500.12110/paper_01666851_v198_n2_p104_Jager
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_version_	1807315132873703424

Identification of novel cyclic nucleotide binding proteins in Trypanosoma cruzi

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