Linking starch metabolism with photosystem I—with PhytoAB antibodies!

Does protein association alone explain how starch metabolism influences photosynthesis?

Ng and colleagues at Washington State University investigated rice plastidial phosphorylase Pho1 and its regulatory L80 region. Catalytically inactive Pho1 variants retained association with the photosystem I subunit PsaC, but failed to reproduce the PSI regulation observed with catalytically active Pho1ΔL80.

These findings indicate that PsaC association alone is insufficient: Pho1 catalytic integrity is required for L80-dependent modulation of photosystem I.

The researchers used PhytoAB’s anti-PsaC antibody, reported as PHY0055A, at a 1:500 dilution for immunoblotting. PsaC detection in co-immunoprecipitation and Halo-tag pulldown experiments helped assess its association with Pho1 variants.

Explore PhytoAB’s PsaC antibody range:

PHY0055A: Anti-PsaC subunit of photosystem I antibody

For the publication-reported PHY0055A reagent and current availability, contact info@phytoab.com.

Studying photosystem I, chloroplast proteins, or starch metabolism? Explore PhytoAB antibodies for your research.

Reference

Ng, C.-Y., Hwang, S.-K., Wood, M., Kirchhoff, H., & Okita, T. W. (2026). Catalytic integrity of plastidial phosphorylase (PHO1) is required for L80-mediated regulation of photosystem I. Journal of Plant Physiology, 326, 154871.