Abstract：
:The nutritional alarmones ppGpp and pppGpp (collectively: (p)ppGpp) are nucleotide-based second messengers enabling bacteria to respond to environmental and stress conditions. Several bacterial species contain two highly homologous (p)ppGpp synthetases named RelP (SAS2, YwaC) and RelQ (SAS1, YjbM). It is established that RelQ forms homotetramers that are subject to positive allosteric regulation by pppGpp, but structural and mechanistic insights into RelP lack behind. Here we present a structural and mechanistic characterization of RelP. In stark contrast to RelQ, RelP is not allosterically regulated by pppGpp and displays a different enzyme kinetic behavior. This discrepancy is evoked by different conformational properties of the guanosine-substrate binding site (G-Loop) of both proteins. Our study shows how minor structural divergences between close homologues result in new functional features during the course of molecular evolution.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Steinchen W,Vogt MS,Altegoer F,Giammarinaro PI,Horvatek P,Wolz C,Bange Gdoi
10.1038/s41598-018-20634-4subject
Has Abstractpub_date
2018-02-01 00:00:00pages
2195issue
1issn
2045-2322pii
10.1038/s41598-018-20634-4journal_volume
8pub_type
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