Abstract

PSI-H is an intrinsic membrane protein of 10 kDa that is a subunit of photosystem I (PSI). PSI-H is one of the three PSI subunits found only in eukaryotes. The function of PSI-H was characterized in Arabidopsis plants transformed with a psaH cDNA in sense orientation. Cosuppressed plants containing less than 3% PSI-H are smaller than wild type when grown on sterile media but are similar to wild type under optimal conditions. PSI complexes lacking PSI-H contain 50% PSI-L, whereas other PSI subunits accumulate in wild type amounts. PSI devoid of PSI-H has only 61% NADP+ photoreduction activity compared with wild type and is highly unstable in the presence of urea as determined from flash-induced absorbance changes at 834 nm. Our data show that PSI-H is required for stable accumulation of PSI and efficient electron transfer in the complex. The plants lacking PSI-H compensate for the less efficient PSI with a 15% increase in the P700/chlorophyll ratio, and this compensation is sufficient to prevent overreduction of the plastoquinone pool as evidenced by normal photochemical quenching of fluorescence. Nonphotochemical quenching is approximately 60% of the wild type value, suggesting that the proton gradient across the thylakoid membrane is decreased in the absence of PSI-H.

Highlights

  • PSI-H is an intrinsic membrane protein of 10 kDa that is a subunit of photosystem I (PSI)

  • PSI-L is essential for formation of PSI trimers in cyanobacteria [7], but plant PSI complexes are not assembled in trimers, and the function of PSI-L in plants is far unsolved

  • The properties of PSI-H combined with the relatively high stability of plant PSI have led us to suggest that the role of the N terminus of PSI-D in stability is mediated through an interaction with the PSI-H subunit [8]

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Summary

Introduction

PSI-H is an intrinsic membrane protein of 10 kDa that is a subunit of photosystem I (PSI). PSI complexes lacking PSI-H contain 50% PSI-L, whereas other PSI subunits accumulate in wild type amounts. Our data show that PSI-H is required for stable accumulation of PSI and efficient electron transfer in the complex. In addition to the 13 subunits of PSI in a narrow sense, plants contain light harvesting complex I (LHCI), which is composed of four different polypeptides, Lhca , that are associated with PSI [1, 2]. Despite the sequence similarities, PSI subunits of cyanobacteria and plants show important functional differences. Because light-harvesting chlorophyll a/bbinding proteins are only present in plants and not in cyanobacteria, an alternative suggestion for the function of PSI-H has been an involvement in the interaction with LHCI [17]. This paper is available on line at http://www.jbc.org thermore, PSI-H is required for interaction with PSI-L, stabilization of FX, and the overall stability of the PSI complex

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