TY - JOUR

T1 - From cyanobacteria to Archaeplastida

T2 - new evolutionary insights into PII signalling in the plant kingdom

AU - Selim, Khaled A.

AU - Ermilova, Elena

AU - Forchhammer, Karl

N1 - Publisher Copyright: © 2020 The Authors New Phytologist © 2020 New Phytologist Trust

PY - 2020/8/1

Y1 - 2020/8/1

N2 - The PII superfamily consists of signal transduction proteins found in all domains of life. Canonical PII proteins sense the cellular energy state through the competitive binding of ATP and ADP, and carbon/nitrogen balance through 2-oxoglutarate binding. The ancestor of Archaeplastida inherited its PII signal transduction protein from an ancestral cyanobacterial endosymbiont. Over the course of evolution, plant PII proteins acquired a glutamine-sensing C-terminal extension, subsequently present in all Chloroplastida PII proteins. The PII proteins of various algal strains (red, green and nonphotosynthetic algae) have been systematically investigated with respect to their sensory and regulatory properties. Comparisons of the PII proteins from different phyla of oxygenic phototrophs (cyanobacteria, red algae, Chlorophyta and higher plants) have yielded insights into their evolutionary conservation vs adaptive properties. The highly conserved role of the controlling enzyme of arginine biosynthesis, N-acetyl-l-glutamate kinase (NAGK), as a main PII-interactor has been demonstrated across oxygenic phototrophs of cyanobacteria and Archaeplastida. In addition, the PII signalling system of red algae has been identified as an evolutionary intermediate between that of Cyanobacteria and Chloroplastida. In this review, we consider recent advances in understanding metabolic signalling by PII proteins of the plant kingdom.

AB - The PII superfamily consists of signal transduction proteins found in all domains of life. Canonical PII proteins sense the cellular energy state through the competitive binding of ATP and ADP, and carbon/nitrogen balance through 2-oxoglutarate binding. The ancestor of Archaeplastida inherited its PII signal transduction protein from an ancestral cyanobacterial endosymbiont. Over the course of evolution, plant PII proteins acquired a glutamine-sensing C-terminal extension, subsequently present in all Chloroplastida PII proteins. The PII proteins of various algal strains (red, green and nonphotosynthetic algae) have been systematically investigated with respect to their sensory and regulatory properties. Comparisons of the PII proteins from different phyla of oxygenic phototrophs (cyanobacteria, red algae, Chlorophyta and higher plants) have yielded insights into their evolutionary conservation vs adaptive properties. The highly conserved role of the controlling enzyme of arginine biosynthesis, N-acetyl-l-glutamate kinase (NAGK), as a main PII-interactor has been demonstrated across oxygenic phototrophs of cyanobacteria and Archaeplastida. In addition, the PII signalling system of red algae has been identified as an evolutionary intermediate between that of Cyanobacteria and Chloroplastida. In this review, we consider recent advances in understanding metabolic signalling by PII proteins of the plant kingdom.

KW - biotin carboxyl carrier protein-subunit of acetyl-CoA carboxylase

KW - cyanobacteria

KW - glutamine sensing

KW - N-acetyl-l-glutamate kinase

KW - PII signalling

KW - plant kingdom

KW - Q-loop

KW - SYMBIOTIC CHLORELLA-VARIABILIS

KW - ARABIDOPSIS-THALIANA PII

KW - N-ACETYLGLUTAMATE-KINASE

KW - P-II

KW - TRANSDUCTION PROTEIN

KW - ARGININE SYNTHESIS

KW - CRYSTAL-STRUCTURE

KW - STRUCTURAL BASIS

KW - NITROGEN

KW - COMPLEX

UR - http://www.scopus.com/inward/record.url?scp=85082759784&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/9a4c62c4-6ea8-31dc-a61d-94ff5f1bae77/

U2 - 10.1111/nph.16492

DO - 10.1111/nph.16492

M3 - Review article

C2 - 32077495

VL - 227

SP - 722

EP - 731

JO - New Phytologist

JF - New Phytologist

SN - 0028-646X

IS - 3

ER -