The Rice Plastidial Phosphorylase Participates Directly in Both Sink and Source Processes. (25th November 2020)

• Record Type: Journal Article
• Authors: Koper, Kaan; Hwang, Seon-Kap; Wood, Magnus; Singh, Salvinder; Cousins, Asaph; Kirchhoff, Helmut; Okita, Thomas W
• Is Part Of: Plant & cell physiology. Volume 62:Number 1(2021)
• Page Start: 125
• Page End: 142
• Publication Date: 2020-11-25
• Subjects: Phosphorylase -- Photosystem I -- PsaC -- Starch; Plant physiology -- Periodicals; Microbiology -- Periodicals; Cytology -- Periodicals; Cell Physiology -- Periodicals; Plant Physiological Phenomena -- Periodicals; Cytology; Microbiology; Plant physiology; Periodicals; 571.205
• DOI: 10.1093/pcp/pcaa146
• Languages: English
• ISSNs: 0032-0781

Abstract

Abstract: The plastidial starch phosphorylase (Pho1) functions in starch metabolism. A distinctive structural feature of the higher Pho1 is a 50–82-amino-acid long peptide (L50–L82), which is absent in phosphorylases from non-plant organisms. To study the function of the rice Pho1 L80 peptide, we complemented a pho1 − rice mutant (BMF136) with the wild-type Pho1 gene or with a Pho1 gene lacking the L80 region (Pho1ΔL80). While expression of Pho1 in BMF136 restored normal wild-type phenotype, the introduction of Pho1ΔL80 enhanced the growth rate and plant productivity above wild-type levels. Mass spectrometry analysis of proteins captured by anti-Pho1 showed the surprising presence of PsaC, the terminal electron acceptor/donor subunit of photosystem I (PSI). This unexpected interaction was substantiated by reciprocal immobilized protein pull-down assays of seedling extracts and supported by the presence of Pho1 on isolated PSI complexes resolved by blue-native gels. Spectrophotometric studies showed that Pho1ΔL80 plants exhibited modified PSI and enhanced CO2 assimilation properties. Collectively, these findings indicate that the higher plant Pho1 has dual roles as a potential modulator of source and sink processes.