Publications
2006
Leontis N B, Lescoute A, Westhof E
The building blocks and motifs of RNA architecture Journal Article
In: Curr Opin Struct Biol, vol. 16, no. 3, pp. 279-287, 2006, ISBN: 16713707, (0959-440X (Print) Journal Article Review).
Abstract | Links | BibTeX | Tags: ase Pairing Base Sequence Computational Biology/methods Conserved Sequence *Models, Extramural Research Support, Molecular Nucleic Acid Conformation RNA/*chemistry Research Support, N.I.H., Non-U.S. Gov't, Unité ARN, WESTHOF
@article{,
title = {The building blocks and motifs of RNA architecture},
author = {N B Leontis and A Lescoute and E Westhof},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16713707},
isbn = {16713707},
year = {2006},
date = {2006-01-01},
journal = {Curr Opin Struct Biol},
volume = {16},
number = {3},
pages = {279-287},
abstract = {RNA motifs can be defined broadly as recurrent structural elements containing multiple intramolecular RNA-RNA interactions, as observed in atomic-resolution RNA structures. They constitute the modular building blocks of RNA architecture, which is organized hierarchically. Recent work has focused on analyzing RNA backbone conformations to identify, define and search for new instances of recurrent motifs in X-ray structures. One current view asserts that recurrent RNA strand segments with characteristic backbone configurations qualify as independent motifs. Other considerations indicate that, to characterize modular motifs, one must take into account the larger structural context of such strand segments. This follows the biologically relevant motivation, which is to identify RNA structural characteristics that are subject to sequence constraints and that thus relate RNA architectures to sequences.},
note = {0959-440X (Print)
Journal Article
Review},
keywords = {ase Pairing Base Sequence Computational Biology/methods Conserved Sequence *Models, Extramural Research Support, Molecular Nucleic Acid Conformation RNA/*chemistry Research Support, N.I.H., Non-U.S. Gov't, Unité ARN, WESTHOF},
pubstate = {published},
tppubtype = {article}
}
2005
Champagne K S, Sissler M, Larrabee Y, Doublie S, Francklyn C S
Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog Journal Article
In: J Biol Chem, vol. 280, no. 40, pp. 34096-34104, 2005, ISBN: 16051603, (0021-9258 (Print) Journal Article).
Abstract | Links | BibTeX | Tags: Extramural Research Support, FLORENTZ ATP Phosphoribosyltransferase/*metabolism Allosteric Regulation Amino Acyl-tRNA Synthetases DNA Mutational Analysis Enzyme Activation *Models, N.I.H., Non-P.H.S. Research Support, P.H.S., SISSLER, Structural Phosphates/metabolism Research Support, U.S. Gov't, Unité ARN
@article{,
title = {Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog},
author = {K S Champagne and M Sissler and Y Larrabee and S Doublie and C S Francklyn},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16051603},
isbn = {16051603},
year = {2005},
date = {2005-01-01},
journal = {J Biol Chem},
volume = {280},
number = {40},
pages = {34096-34104},
abstract = {ATP phosphoribosyl transferase (ATP-PRT) joins ATP and 5-phosphoribosyl-1-pyrophosphate (PRPP) in a highly regulated reaction that initiates histidine biosynthesis. The unusual hetero-octameric version of ATP-PRT includes four HisG(S) catalytic subunits based on the periplasmic binding protein fold and four HisZ regulatory subunits that resemble histidyl-tRNA synthetases. Here, we present the first structure of a PRPP-bound ATP-PRT at 2.9 A and provide a structural model for allosteric activation based on comparisons with other inhibited and activated ATP-PRTs from both the hetero-octameric and hexameric families. The activated state of the octameric enzyme is characterized by an interstitial phosphate ion in the HisZ-HisG interface and new contacts between the HisZ motif 2 loop and the HisG(S) dimer interface. These contacts restructure the interface to recruit conserved residues to the active site, where they activate pyrophosphate to promote catalysis. Additionally, mutational analysis identifies the histidine binding sites within a region highly conserved between HisZ and the functional HisRS. Through the oligomerization and functional re-assignment of protein domains associated with aminoacylation and phosphate binding, the HisZ-HisG octameric ATP-PRT acquired the ability to initiate the synthesis of a key metabolic intermediate in an allosterically regulated fashion.},
note = {0021-9258 (Print)
Journal Article},
keywords = {Extramural Research Support, FLORENTZ ATP Phosphoribosyltransferase/*metabolism Allosteric Regulation Amino Acyl-tRNA Synthetases DNA Mutational Analysis Enzyme Activation *Models, N.I.H., Non-P.H.S. Research Support, P.H.S., SISSLER, Structural Phosphates/metabolism Research Support, U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Castellano S, Lobanov A V, Chapple C, Novoselov S V, Albrecht M, Hua D, Lescure A, Lengauer T, Krol A, Gladyshev V N, Guigo R
Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family Journal Article
In: Proc Natl Acad Sci U S A, vol. 102, no. 45, pp. 16188-16193, 2005, ISBN: 16260744, (0027-8424 (Print) Journal Article).
Abstract | Links | BibTeX | Tags: Extramural Research Support, KROL Adenosine Diphosphate Ribose/metabolism Animals Fish Proteins/chemistry/genetics/*physiology Genome Mice NIH 3T3 Cells Phylogeny Promoter Regions (Genetics) Proteome Research Support, LESCURE, N.I.H., Non-P.H.S. Selenoproteins/chemistry/genetics/*physiology Tetraodontiformes/*genetics, Non-U.S. Gov't Research Support, U.S. Gov't, Unité ARN
@article{,
title = {Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family},
author = {S Castellano and A V Lobanov and C Chapple and S V Novoselov and M Albrecht and D Hua and A Lescure and T Lengauer and A Krol and V N Gladyshev and R Guigo},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16260744},
isbn = {16260744},
year = {2005},
date = {2005-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {102},
number = {45},
pages = {16188-16193},
abstract = {Selenoproteins are a diverse group of proteins that contain selenocysteine (Sec), the 21st amino acid. In the genetic code, UGA serves as a termination signal and a Sec codon. This dual role has precluded the automatic annotation of selenoproteins. Recent advances in the computational identification of selenoprotein genes have provided a first glimpse of the size, functions, and phylogenetic diversity of eukaryotic selenoproteomes. Here, we describe the identification of a selenoprotein family named SelJ. In contrast to known selenoproteins, SelJ appears to be restricted to actinopterygian fishes and sea urchin, with Cys homologues only found in cnidarians. SelJ shows significant similarity to the jellyfish J1-crystallins and with them constitutes a distinct subfamily within the large family of ADP-ribosylation enzymes. Consistent with its potential role as a structural crystallin, SelJ has preferential and homogeneous expression in the eye lens in early stages of zebrafish development. A structural role for SelJ would be in contrast to the majority of known selenoenzymes. The unusually highly restricted phylogenetic distribution of SelJ, its specialization, and the comparative analysis of eukaryotic selenoproteomes reveal the diversity and functional plasticity of selenoproteins and point to a mosaic evolution of the use of Sec in proteins.},
note = {0027-8424 (Print)
Journal Article},
keywords = {Extramural Research Support, KROL Adenosine Diphosphate Ribose/metabolism Animals Fish Proteins/chemistry/genetics/*physiology Genome Mice NIH 3T3 Cells Phylogeny Promoter Regions (Genetics) Proteome Research Support, LESCURE, N.I.H., Non-P.H.S. Selenoproteins/chemistry/genetics/*physiology Tetraodontiformes/*genetics, Non-U.S. Gov't Research Support, U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}