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Title: Structural and Functional Perturbation of Giardia lamblia Triosephosphate Isomerase by Modification of a Non- Catalytic, Non-Conserved Region

Authors:
; ; ; ; ; ; ; ; ; ; ; ; ; ; ;  [1];  [2]
  1. (INP-Mexico)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
FOREIGN
OSTI Identifier:
1140260
Resource Type:
Journal Article
Resource Relation:
Journal Name: PLoS One; Journal Volume: 8; Journal Issue: (7) ; 07, 2014
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Hernandez-Alcantara, Gloria, Torres-Lario, Alfredo, Enr, #305, quez-Flo, Sergio, Garc, #305, a-Torres, Itzhel, Castillo-Villanueva, Adriana, Mendez, Sara T., de la Mora-de la Mora, Ignacio, Gomez-Manzo, Saul, Torres-Arroyo, Angelica, Lopez-Velazquez, Gabriel, Reyes-Vivas, Horacio, Oria-Hernandez, Jesus, and UNAM-Mexico). Structural and Functional Perturbation of Giardia lamblia Triosephosphate Isomerase by Modification of a Non- Catalytic, Non-Conserved Region. United States: N. p., 2014. Web. doi:10.1371/journal.pone.0069031.
Hernandez-Alcantara, Gloria, Torres-Lario, Alfredo, Enr, #305, quez-Flo, Sergio, Garc, #305, a-Torres, Itzhel, Castillo-Villanueva, Adriana, Mendez, Sara T., de la Mora-de la Mora, Ignacio, Gomez-Manzo, Saul, Torres-Arroyo, Angelica, Lopez-Velazquez, Gabriel, Reyes-Vivas, Horacio, Oria-Hernandez, Jesus, & UNAM-Mexico). Structural and Functional Perturbation of Giardia lamblia Triosephosphate Isomerase by Modification of a Non- Catalytic, Non-Conserved Region. United States. doi:10.1371/journal.pone.0069031.
Hernandez-Alcantara, Gloria, Torres-Lario, Alfredo, Enr, #305, quez-Flo, Sergio, Garc, #305, a-Torres, Itzhel, Castillo-Villanueva, Adriana, Mendez, Sara T., de la Mora-de la Mora, Ignacio, Gomez-Manzo, Saul, Torres-Arroyo, Angelica, Lopez-Velazquez, Gabriel, Reyes-Vivas, Horacio, Oria-Hernandez, Jesus, and UNAM-Mexico). Thu . "Structural and Functional Perturbation of Giardia lamblia Triosephosphate Isomerase by Modification of a Non- Catalytic, Non-Conserved Region". United States. doi:10.1371/journal.pone.0069031.
@article{osti_1140260,
title = {Structural and Functional Perturbation of Giardia lamblia Triosephosphate Isomerase by Modification of a Non- Catalytic, Non-Conserved Region},
author = {Hernandez-Alcantara, Gloria and Torres-Lario, Alfredo and Enr and #305 and quez-Flo, Sergio and Garc and #305 and a-Torres, Itzhel and Castillo-Villanueva, Adriana and Mendez, Sara T. and de la Mora-de la Mora, Ignacio and Gomez-Manzo, Saul and Torres-Arroyo, Angelica and Lopez-Velazquez, Gabriel and Reyes-Vivas, Horacio and Oria-Hernandez, Jesus and UNAM-Mexico)},
abstractNote = {},
doi = {10.1371/journal.pone.0069031},
journal = {PLoS One},
number = (7) ; 07, 2014,
volume = 8,
place = {United States},
year = {Thu Aug 14 00:00:00 EDT 2014},
month = {Thu Aug 14 00:00:00 EDT 2014}
}
  • Box C/D ribonucleoproteins (RNP) guide the 2'-O-methylation of targeted nucleotides in archaeal and eukaryotic rRNAs. The archaeal L7Ae and eukaryotic 15.5kD box C/D RNP core protein homologues initiate RNP assembly by recognizing kink-turn (K-turn) motifs. The crystal structure of the 15.5kD core protein from the primitive eukaryote Giardia lamblia is described here to a resolution of 1.8 {angstrom}. The Giardia 15.5kD protein exhibits the typical {alpha}-{beta}-{alpha} sandwich fold exhibited by both archaeal L7Ae and eukaryotic 15.5kD proteins. Characteristic of eukaryotic homologues, the Giardia 15.5kD protein binds the K-turn motif but not the variant K-loop motif. The highly conserved residues ofmore » loop 9, critical for RNA binding, also exhibit conformations similar to those of the human 15.5kD protein when bound to the K-turn motif. However, comparative sequence analysis indicated a distinct evolutionary position between Archaea and Eukarya. Indeed, assessment of the Giardia 15.5kD protein in denaturing experiments demonstrated an intermediate stability in protein structure when compared with that of the eukaryotic mouse 15.5kD and archaeal Methanocaldococcus jannaschii L7Ae proteins. Most notable was the ability of the Giardia 15.5kD protein to assemble in vitro a catalytically active chimeric box C/D RNP utilizing the archaeal M. jannaschii Nop56/58 and fibrillarin core proteins. In contrast, a catalytically competent chimeric RNP could not be assembled using the mouse 15.5kD protein. Collectively, these analyses suggest that the G. lamblia 15.5kD protein occupies a unique position in the evolution of this box C/D RNP core protein retaining structural and functional features characteristic of both archaeal L7Ae and higher eukaryotic 15.5kD homologues.« less
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