Results 241 to 250 of about 26,255 (351)

BacExplorer: an integrated platform for <i>de novo</i> bacterial genome annotation. [PDF]

open access: yesBioinform Adv
Privitera GF   +5 more
europepmc   +1 more source

A short peptide derived from late embryogenesis abundant proteins enhances acid tolerance in Escherichia coli via modulation of two‐component regulatory systems

open access: yesThe FEBS Journal, EarlyView.
Expression of the LEA‐K peptide in E. coli BL21 (DE3) improved bacterial viability under acidic stress (pH4), suggesting a protective function. RNA‐sequencing of LEA‐K‐expressing vs. non‐expressing cells revealed 283 differentially expressed genes (DEGs). In silico docking linked LEA‐K to two‐component systems (TCS) proteins (Rcs, BtsS/R, and EnvZ/OmpR)
Khaled Metwally, Shinya Ikeno
wiley   +1 more source

Heterologous plastoquinone production using a newly identified O2‐dependent cyanobacterial hydroxylase

open access: yesThe FEBS Journal, EarlyView.
In this study, we confirm that PlqH is the hydroxylase operating in plastoquinone biosynthesis in photosynthetic cyanobacteria (Cyanobacteriia). Our phylogenetic analyses demonstrate that cyanobacterial PlqH homologues originated from hydroxylases involved in ubiquinone biosynthesis in bacteria. Plastoquinone production in Escherichia coli was achieved
Morgane Roger‐Margueritat   +7 more
wiley   +1 more source

Bacteriophage Typing of Methicillin Resistant Staphylococcus aureus and Changing Trend in their Antibiotic Profile

open access: diamond, 2016
Abarna Velayudham   +4 more
openalex   +1 more source

Binding of Bacillus subtilis dynamin‐like protein DynA to the bacterial membrane is essential for effective phage defense

open access: yesThe FEBS Journal, EarlyView.
The bacterial dynamin‐like protein DynA from Bacillus subtilis plays a key role in phage defense. It binds the plasma membrane through a unique paddle domain in its D1 subunit. This membrane association is essential for its protective function, likely preventing explosive membrane rupture following phage infection.
Samia Shafqat   +2 more
wiley   +1 more source

Investigating the molecular mechanisms underlying the anti‐CRISPR function of AcrIIA13b protein

open access: yesThe FEBS Journal, EarlyView.
Anti‐CRISPR protein AcrIIA13b inhibits CRISPR–Cas9 function by preventing target DNA engagement. The Cas9–sgRNA ribonucleoprotein (RNP) normally recognizes the protospacer adjacent motif (PAM) duplex to initiate DNA cleavage. AcrIIA13b binding to the PAM‐interacting WED–PI domain blocks this recognition, leaving the target DNA intact.
So Yeon Lee, Hyun Ho Park
wiley   +1 more source

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