Results 121 to 130 of about 60,289 (232)

Warming Causes a Decline in Baltic Sea Coastal Sediment Microbial Abundance. [PDF]

open access: yesEnviron Microbiol
Long‐term warming in the Baltic Sea coastal area has led to a decrease in sediment microbial cell abundance, alongside a shallowing of sediment biogeochemical zones and associated microbial communities. These changes may become more pronounced in marine sediments under future climate change‐related warming.
Seidel L   +8 more
europepmc   +2 more sources

Fluorescence-based incision assay for human XPF-ERCC1 activity identifies important elements of DNA junction recognition [PDF]

open access: yes, 2012
The structure-specific endonuclease activity of the human XPF–ERCC1 complex is essential for a number of DNA processing mechanisms that help to maintain genomic integrity.
Bowles, M.   +5 more
core   +1 more source

Deciphering the properties and reaction mechanism of anhydromevalonate phosphate decarboxylase, a prenylated flavin mononucleotide‐dependent enzyme in the archaeal mevalonate pathway

open access: yesThe FEBS Journal, EarlyView.
Characterization of anhydromevalonate phosphate decarboxylase, the UbiD‐family decarboxylase involved in the archaeal mevalonate pathway, was conducted. The enzyme is responsible for the biosynthesis of isoprenoids, such as archaeal membrane lipids, respiratory quinones, and dolichols.
Rino Ishikawa   +9 more
wiley   +1 more source

H2‐dependent modulation of tetrahydromethanopterin S‐methyltransferase (Mtr complex) activity by the small protein MtrR in Methanosarcina mazei

open access: yesThe FEBS Journal, EarlyView.
Small protein MtrR is a regulator of the Mtr methyltransferase complex in Methanosarcina mazei. It binds specifically to the MtrA subunit and modulates Mtr activity in response to hydrogen (H2) availability. Deleting mtrR impairs growth in the presence but not absence of H2, indicating its role in directing methyl transfer toward an energy‐conserving ...
Tim Habenicht   +6 more
wiley   +1 more source

Archaeal TFEα/β is a hybrid of TFIIE and the RNA polymerase III subcomplex hRPC62/39

open access: yeseLife, 2015
Transcription initiation of archaeal RNA polymerase (RNAP) and eukaryotic RNAPII is assisted by conserved basal transcription factors. The eukaryotic transcription factor TFIIE consists of α and β subunits.
Fabian Blombach   +10 more
doaj   +1 more source

ESCRT-III mediated cell division in Sulfolobus acidocaldarius - a reconstitution perspective [PDF]

open access: yes, 2014
In the framework of synthetic biology, it has become an intriguing question what would be the minimal representation of cell division machinery. Thus, it seems appropriate to compare how cell division is realized in different microorganisms. Inparticular,
Härtel, T., Schwille, P.
core   +2 more sources

Antioxidative and chaperone‐like activities of a bacterioruberin‐rich extract: An innovative approach to protect the skin proteome

open access: yesInternational Journal of Cosmetic Science, EarlyView.
The bacteriorubin‐rich extract of Arthrobacter agilis has high antioxidative properties, protecting proteins against oxidative stress and preventing their carbonylation. It also protects proteins against saline and heat stresses, suggesting a dual mode of action including antioxidant and chaperone‐like activities.
Julie C. Tisserand   +7 more
wiley   +1 more source

Genomic Inference of the Metabolism and Evolution of the Archaeal Phylum Aigarchaeota [PDF]

open access: yes, 2018
Microbes of the phylum Aigarchaeota are widely distributed in geothermal environments, but their physiological and ecological roles are poorly understood.
Castelle, Cindy J.   +14 more
core   +3 more sources

Bacillus subtilis RNase HII Is Inefficient at Processing Guanosine Monophosphate and Damaged Ribonucleotides

open access: yesMolecular Microbiology, EarlyView.
Bacillus subtilis RNase HII corrects ribonucleotide errors and mismatched ribonucleotides, but not damaged ribonucleotides. Mismatched ribonucleotides would also serve as substrates for mismatch repair while damaged ribonucleotides would be addressed through base excision repair.
Julianna R. Cresti, Lyle A. Simmons
wiley   +1 more source

The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain

open access: yesBiology Direct, 2010
Primase and GINS are essential factors for chromosomal DNA replication in eukaryotic and archaeal cells. Here we describe a previously undetected relationship between the C-terminal domain of the catalytic subunit (PriS) of archaeal primase and the B ...
Swiatek Agnieszka, MacNeill Stuart A
doaj   +1 more source

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