Collaboration Between CC- and A-Adding Enzymes to Build and Repair the 3'-Terminal CCA of tRNA in Aquifex aeolicus

Science ◽  
2001 ◽  
Vol 294 (5545) ◽  
pp. 1334-1336 ◽  
Author(s):  
K. Tomita
Keyword(s):  
Aquifex Aeolicus

Exemplar Abstract for Aquifex aeolicus Huber and Stetter 2001.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Aquifex Aeolicus

Nomenclature Abstract for Aquifex aeolicus Huber and Stetter 2001.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Aquifex Aeolicus

The hyperthermophilic nature of the metallo-oxidase from Aquifex aeolicus

2009 ◽  
Vol 1794 (1) ◽  
pp. 75-83 ◽  
Author(s):  
André T. Fernandes ◽  
Lígia O. Martins ◽  
Eduardo P. Melo
Keyword(s):  
Aquifex Aeolicus

A naturally occurring nonapeptide functionally compensates for the CP1 domain of leucyl-tRNA synthetase to modulate aminoacylation activity

2012 ◽  
Vol 443 (2) ◽  
pp. 477-484 ◽  
Author(s):  
Min Tan ◽  
Wei Yan ◽  
Ru-Juan Liu ◽  
Meng Wang ◽  
Xin Chen ◽  
...  
Keyword(s):  
Catalytic Efficiency ◽  
Trna Synthetase ◽  
Modular Construction ◽  
Aquifex Aeolicus ◽  
Trna Synthetases ◽  
Naturally Occurring ◽  
Aminoacyl Trna Synthetases ◽  
Editing Domain ◽  
Editing Activity ◽  
Shed Light

aaRSs (aminoacyl-tRNA synthetases) establish the rules of the genetic code by catalysing the formation of aminoacyl-tRNA. The quality control for aminoacylation is achieved by editing activity, which is usually carried out by a discrete editing domain. For LeuRS (leucyl-tRNA synthetase), the CP1 (connective peptide 1) domain is the editing domain responsible for hydrolysing mischarged tRNA. The CP1 domain is universally present in LeuRSs, except MmLeuRS (Mycoplasma mobile LeuRS). The substitute of CP1 in MmLeuRS is a nonapeptide (MmLinker). In the present study, we show that the MmLinker, which is critical for the aminoacylation activity of MmLeuRS, could confer remarkable tRNA-charging activity on the inactive CP1-deleted LeuRS from Escherichia coli (EcLeuRS) and Aquifex aeolicus (AaLeuRS). Furthermore, CP1 from EcLeuRS could functionally compensate for the MmLinker and endow MmLeuRS with post-transfer editing capability. These investigations provide a mechanistic framework for the modular construction of aaRSs and their co-ordination to achieve catalytic efficiency and fidelity. These results also show that the pre-transfer editing function of LeuRS originates from its conserved synthetic domain and shed light on future study of the mechanism.

scholarly journals Crystal structure and RNA-binding properties of an Hfq homolog from the deep-branching Aquificae: conservation of the lateral RNA-binding mode

2017 ◽  
Vol 73 (4) ◽  
pp. 294-315 ◽  
Author(s):  
Kimberly A. Stanek ◽  
Jennifer Patterson-West ◽  
Peter S. Randolph ◽  
Cameron Mura
Keyword(s):  
Rna Binding ◽  
Binding Pocket ◽  
Binding Mode ◽  
Evolutionary Conservation ◽  
Aquifex Aeolicus ◽  
Binding Properties ◽  
Bacterial Phyla ◽  
Mrna Targets ◽  
Small Regulatory Rnas ◽  
And Function

The host factor Hfq, as the bacterial branch of the Sm family, is an RNA-binding protein involved in the post-transcriptional regulation of mRNA expression and turnover. Hfq facilitates pairing between small regulatory RNAs (sRNAs) and their corresponding mRNA targets by binding both RNAs and bringing them into close proximity. Hfq homologs self-assemble into homo-hexameric rings with at least two distinct surfaces that bind RNA. Recently, another binding site, dubbed the `lateral rim', has been implicated in sRNA·mRNA annealing; the RNA-binding properties of this site appear to be rather subtle, and its degree of evolutionary conservation is unknown. An Hfq homolog has been identified in the phylogenetically deep-branching thermophileAquifex aeolicus(Aae), but little is known about the structure and function of Hfq from basal bacterial lineages such as the Aquificae. Therefore,AaeHfq was cloned, overexpressed, purified, crystallized and biochemically characterized. Structures ofAaeHfq were determined in space groupsP1 andP6, both to 1.5 Å resolution, and nanomolar-scale binding affinities for uridine- and adenosine-rich RNAs were discovered. Co-crystallization with U6RNA reveals that the outer rim of theAaeHfq hexamer features a well defined binding pocket that is selective for uracil. ThisAaeHfq structure, combined with biochemical and biophysical characterization of the homolog, reveals deep evolutionary conservation of the lateral RNA-binding mode, and lays a foundation for further studies of Hfq-associated RNA biology in ancient bacterial phyla.

Insights on a New PDI-like Family: Structural and Functional Analysis of a Protein Disulfide Oxidoreductase from the Bacterium Aquifex aeolicus

2006 ◽  
Vol 356 (1) ◽  
pp. 155-164 ◽  
Author(s):  
Emilia Pedone ◽  
Katia D'Ambrosio ◽  
Giuseppina De Simone ◽  
Mosè Rossi ◽  
Carlo Pedone ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Aquifex Aeolicus ◽  
Protein Disulfide Oxidoreductase ◽  
Disulfide Oxidoreductase ◽  
Protein Disulfide

scholarly journals A new sulfurtransferase from the hyperthermophilic bacterium Aquifex aeolicus

FEBS Journal ◽  
2007 ◽  
Vol 274 (17) ◽  
pp. 4572-4587 ◽  
Author(s):  
Marie-Cécile Giuliani ◽  
Pascale Tron ◽  
Gisèle Leroy ◽  
Corinne Aubert ◽  
Patrick Tauc ◽  
...  
Keyword(s):  
Aquifex Aeolicus ◽  
Hyperthermophilic Bacterium
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