Results 51 to 60 of about 5,022 (174)

A Novel Polyphosphate‐Degrading Enzyme Confers Growth on Exogenous Polyphosphate in the Archaeon Haloferax volcanii

open access: yesEnvironmental Microbiology, Volume 28, Issue 7, July 2026.
A novel polyP‐degrading enzyme with an activity differing from those currently known was found in Haloferax volcanii, conferring the ability for this microbe to grow on extracellular polyP. These findings further our understanding of the potential ecological roles of polyP and how archaea metabolise this essential biopolymer.
Jack W. F. Nicholls   +4 more
wiley   +1 more source

Structure of the heterotrimeric PCNA fromSulfolobus solfataricus [PDF]

open access: yesActa Crystallographica Section F Structural Biology and Crystallization Communications, 2006
PCNA is a ring-shaped protein that encircles DNA, providing a platform for the association of a wide variety of DNA-processing enzymes that utilize the PCNA sliding clamp to maintain proximity to their DNA substrates. PCNA is a homotrimer in eukaryotes, but a heterotrimer in crenarchaea such as Sulfolobus solfataricus.
Williams, Gareth J.   +9 more
openaire   +2 more sources

Is a Malleable Active Site Loop the Key to High Substrate Promiscuity? Hybrid, Biocatalytic Route to Structurally Diverse Taxoid Side Chains with Remarkable Dual Stereocontrol

open access: yesAngewandte Chemie, Volume 137, Issue 36, September 1, 2025.
A highly stereoselective, dynamic reductive kinetic resolution (DYRKR) entry into myriad Taxotere‐like side chains with Clostridium acetobutylicum alcohol dehydrogenase (CaADH) enzyme is reported. Follow‐on cross couplings expand the structural diversity of the library (36 total examples).
Gaurav P. Kudalkar   +15 more
wiley   +2 more sources

Efficient CRISPR-Mediated Post-Transcriptional Gene Silencing in a Hyperthermophilic Archaeon Using Multiplexed crRNA Expression

open access: yesG3: Genes, Genomes, Genetics, 2016
CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats)-mediated RNA degradation is catalyzed by a type III system in the hyperthermophilic archaeon Sulfolobus solfataricus. Earlier work demonstrated that the system can be engineered to target
Ziga Zebec   +3 more
doaj   +1 more source

The Role of Polyphosphate in Motility, Adhesion, and Biofilm Formation in Sulfolobales

open access: yesMicroorganisms, 2021
Polyphosphates (polyP) are polymers of orthophosphate residues linked by high-energy phosphoanhydride bonds that are important in all domains of life and function in many different processes, including biofilm development. To study the effect of polyP in
Alejandra Recalde   +5 more
doaj   +1 more source

An Autonomously Replicating Transforming Vector for Sulfolobus solfataricus [PDF]

open access: yesJournal of Bacteriology, 1998
ABSTRACT A plasmid able to transform and to be stably maintained both in Sulfolobus solfataricus and in Escherichia coli was constructed by insertion into an E. coli plasmid of the autonomously replicating sequence of the virus particle SSV1 and a suitable ...
R. Cannio   +3 more
openaire   +5 more sources

Snapshots of Motion: A Novel Structural Intermediate Reveals Conserved Dynamics in Archaeal DNA Ligases

open access: yesProteins: Structure, Function, and Bioinformatics, Volume 94, Issue 6, Page 1245-1258, June 2026.
ABSTRACT We present the first x‐ray crystallographic structural evidence of an archaeal DNA ligase showing the AMP covalent adduct together with further cofactor hydrolysis, capturing a transient intermediary in the first step of the ligation reaction, triggered by the pyrophosphate hydrolysis.
A. X. Quintana‐Armas   +3 more
wiley   +1 more source

Molecular analysis of 3D domain swapping in the acylphosphatase from Escherichia coli

open access: yesActa Crystallographica Section D, Volume 82, Issue 4, Page 336-347, April 2026.
Structures of the monomer and intertwined dimer of the acylphosphatase from E. coli shed light on the molecular basis of its 3D domain swapping.Three‐dimensional domain swapping is a mechanism by which proteins form oligomers. At present, the molecular basis that dictates whether some proteins fold in their monomeric form or as intertwined oligomers is
Sergio Martínez-Rodríguez   +4 more
wiley   +1 more source

Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring. [PDF]

open access: yesPLoS ONE, 2010
The exosome complex is an essential RNA 3'-end processing and degradation machinery. In archaeal organisms, the exosome consists of a catalytic ring and an RNA-binding ring, both of which were previously reported to assume three-fold symmetry.Here we ...
Changrui Lu, Fang Ding, Ailong Ke
doaj   +1 more source

The return of metabolism: biochemistry and physiology of glycolysis

open access: yesBiological Reviews, Volume 101, Issue 2, Page 751-803, April 2026.
ABSTRACT Glycolysis is a fundamental metabolic pathway central to the bioenergetics and physiology of virtually all living organisms. In this comprehensive review, we explore the intricate biochemical principles and evolutionary origins of glycolytic pathways, from the classical Embden–Meyerhof–Parnas (EMP) pathway in humans to various prokaryotic and ...
Nana‐Maria Grüning   +19 more
wiley   +1 more source

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