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Профиль

artemisaev

Профиль Vively
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Everything phage biology and bacterial immunity Assistant professor at Skoltech, Russia

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Thrilled to share! We present the structure of a prototypical P2 OLD and reveal that its tRNAse activity is triggered by ssDNA hairpins in phage origins or unresolved termini in RecBCD-deficient cells. Great team effort with Wang, Bikard & Nudler labs. www.biorxiv.org/content/10.6...

OLD sentinel: an abortive tRNase surveys phage replication and DNA defects in RecBCD-compromised cellsOLD, an abortive immunity protein from prophage P2, consists of an ABC ATPase sensor and a TO-PRIM nuclease effector - a core architecture shared by a large protein family, including components of ant...www.biorxiv.org
13217
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Happy to share a preview of recent work from E. Koonin & colleagues, revealing the widespread presence of reparative helicases as central components of prokaryotic immune systems. Written by our talented PhD student Oksana. www.cell.com/cell-host-mi...

A repair helicase unravels the tangled web of bacterial immunityDNA repair proteins are repeatedly repurposed for antiviral immunity. In this issue of Cell Host & Microbe, Bell et al. utilized phylogenetic reconstruction of the evolutionary routes of the YprA repa...www.cell.com
071
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The CRISPR-Cas system in E. coli K-12 is considered inactive. We questioned whether mobile elements encode anti-CRISPRs against this system and found a highly abundant AcrIE9-AcrIE10 tandem and a novel AcrIE13 — an HTH protein more similar to Aca than known Acrs. www.pnas.org/doi/10.1073/...

A census of anti-CRISPR proteins reveals AcrIE9 and AcrIE13 as inhibitors of the Escherichia coli K12 type IE CRISPR-Cas system | PNASCRISPR-Cas adaptive immunity systems provide defense against mobile genetic elements and are often countered by diverse anti-CRISPR (Acr) proteins....www.pnas.org
0175
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Some gut commensals are not what they look like. E. coli HS borrows a capsule from Klebsiella, boosting its phage resistance. We also uncovered tail-spike exchanges between phages of different morphotypes and a P22 with dual TSP architecture. www.biorxiv.org/content/10.6...

www.biorxiv.org
051
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SH3 domains are known as cell-wall binding endolysin subunits, conferring host specificity in phages of Gram-positive bacteria. We report that SH3 is also conserved in the cell lysis module of T1-like phages infecting Gram-negative E. coli. www.mdpi.com/1422-0067/27...

www.mdpi.com
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