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

