6NE8

Solution Structure of the Thioredoxin-like Domain of Arabidopsis NCP (NUCLEAR CONTROL OF PEP ACTIVITY)

Summary for 6NE8

• Entry DOI: 10.2210/pdb6ne8/pdb
• NMR Information: BMRB: 30551
• Descriptor: Thioredoxin-like fold domain-containing protein MRL7L, chloroplastic (1 entity in total)
• Functional Keywords: ncp, nuclear control of pep activity, thioredoxin-like domain, chloroplast biogenesis, phytochrome signaling, plastid-encoded rna polymerase, plant protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 1
• Total formula weight: 16605.23

Authors

Liu, J.,Chen, M.,Zhou, P. (deposition date: 2018-12-17, release date: 2019-12-25, Last modification date: 2024-05-15)

Primary citation

Yang, E.J.,Yoo, C.Y.,Liu, J.,Wang, H.,Cao, J.,Li, F.W.,Pryer, K.M.,Sun, T.P.,Weigel, D.,Zhou, P.,Chen, M.
NCP activates chloroplast transcription by controlling phytochrome-dependent dual nuclear and plastidial switches.
Nat Commun, 10:2630-2630, 2019

PubMed Abstract: Phytochromes initiate chloroplast biogenesis by activating genes encoding the photosynthetic apparatus, including photosynthesis-associated plastid-encoded genes (PhAPGs). PhAPGs are transcribed by a bacterial-type RNA polymerase (PEP), but how phytochromes in the nucleus activate chloroplast gene expression remains enigmatic. We report here a forward genetic screen in Arabidopsis that identified NUCLEAR CONTROL OF PEP ACTIVITY (NCP) as a necessary component of phytochrome signaling for PhAPG activation. NCP is dual-targeted to plastids and the nucleus. While nuclear NCP mediates the degradation of two repressors of chloroplast biogenesis, PIF1 and PIF3, NCP in plastids promotes the assembly of the PEP complex for PhAPG transcription. NCP and its paralog RCB are non-catalytic thioredoxin-like proteins that diverged in seed plants to adopt nonredundant functions in phytochrome signaling. These results support a model in which phytochromes control PhAPG expression through light-dependent double nuclear and plastidial switches that are linked by evolutionarily conserved and dual-localized regulatory proteins.

PubMed: 31201314
DOI: 10.1038/s41467-019-10517-1

Experimental method

SOLUTION NMR