English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

“Plus ca change, plus c’est la meme chose” (the more things change, the more they stay the same). Nowhere is this more apparent than in biology, where nature cleverly recycles and adapts the same chemical reactions to control complex physiology from bacteria to archaea, plants, and metazoans (1, 2). However, those of us who work on protein phosphorylation have been lured into thinking bacteria do it one way and the rest of nature another. It has been over 60 years since Fischer and Krebs (3) worked out the basic mechanisms of protein phosphorylation, 35 years since Tony Hunter connected tyrosine phosphorylation to oncogenesis (4), and 25 years since Susan Taylor gave us the iconic protein kinase fold (5). Structural genomic analyses have defined approaching 550 members of the protein kinase superfamily in humans and a burgeoning cohort of pseudokinases (1). This latter group look like their active counterparts but function as allosteric modulators or as enzyme scaffolds (6). So, it seems as if we know it all. However, an article published in PNAS (7) revealing the importance of bacterial Ser and Thr protein kinases in the phosphorylation of spore coat proteins may have begun a new chapter in the protein phosphorylation saga.Regardless of their function, all archaea, plant, and metazoan kinases have evolved to enable the transfer a molecule of phosphate from ATP onto the hydroxyl of Ser, Thr, and Tyr residues. Conversely, bacterial protein kinases are traditionally considered to modify the imidazole of histidine residues on proteins as part of a two-component system. Nevertheless, a few bacterial Ser and Thr kinases were identified, but these enzymes were considered to be esoteric and were often relegated to annals of intellectual curiosity. However, Vincent Tagliabracci and Jack Dixon, who are among the authors of the study published in PNAS … [↵][1]1To whom correspondence should be addressed. Email: scottjdw{at}uw.edu. [1]: #xref-corresp-1-1

Bacterial spore coat protein kinases: A new twist to an old story