The thylakoid protein BCM1 sequesters antennae protein CP24 and CP29 within the grana cores thereby reducing their exposure to degradation under heat stress.

Photosystem II (PSII) is one of the most thermosensitive components of photosynthetic apparatus in higher plants. Heat-inactivation of PSII may be followed by dissociation of antenna proteins, however, the fate and regulation mechanism of detached antenna proteins during this process remains unclear. Here, we investigate the regulation mechanism of two minor antenna proteins CP24 and CP29 during heat acclimation via the study on a thylakoid protein BCM1. BCM1 is distributed in both grana cores (GC) and stroma lamellae of thylakoids. However, heat stress induced its accumulation in grana cores but not stroma lamellae. Deficiency of BCM1 leads to the decline of plant resilience to heat stress, which results from the accelerated degradation of CP24 and CP29 in vivo. Heat stress induces a redistribution of CP24 and CP29 from the grana cores to the stroma lamellae, a shift that is exacerbated in bcm1 mutants, suggesting that migration of detached antennae proteins between thylakoid subcompartments may contribute to their degradation during heat acclimation. As an integral thylakoid protein, BCM1 physically interacts with CP24 and CP29. We propose that BCM1 serves as a stabilizing "anchor", effectively sequestering CP24 and CP29 within the grana cores thereby reducing their exposure to degradation in the stroma lamellae.