2003
DOI: 10.1074/jbc.m305106200
|View full text |Cite
|
Sign up to set email alerts
|

Arabidopsis thaliana Plants Lacking the PSI-D Subunit of Photosystem I Suffer Severe Photoinhibition, Have Unstable Photosystem I Complexes, and Altered Redox Homeostasis in the Chloroplast Stroma

Abstract: The PSI-D subunit of photosystem I is a hydrophilic subunit of about 18 kDa, which is exposed to the stroma and has an important function in the docking of ferredoxin to photosystem I. We have used an antisense approach to obtain Arabidopsis thaliana plants with only 5-60% of PSI-D. No plants were recovered completely lacking PSI-D, suggesting that PSI-D is essential for a functional PSI in plants. Plants with reduced amounts of PSI-D showed a similar decrease in all other subunits of PSI including the light h… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

5
53
0

Year Published

2004
2004
2022
2022

Publication Types

Select...
5
4
1

Relationship

1
9

Authors

Journals

citations
Cited by 62 publications
(58 citation statements)
references
References 72 publications
5
53
0
Order By: Relevance
“…In general, PSI is known to be much more stable, also at high temperatures, than PSII (Berry and Bjö rkman, 1980;Takeuchi and Thornber, 1994;Al-Khatib and Paulsen, 1999), but in the CL3 mutant PSI was more affected than PSII. The biochemical, spectroscopic, and physiological phenotype resembles that described for several other PSI mutants, where the amount of PSI is decreased and a secondary damage to PSII and other thylakoid proteins is observed especially at higher light intensity and with light that predominantly excites PSII (Haldrup et al, 2000(Haldrup et al, , 2003.…”
Section: Discussionmentioning
confidence: 64%
“…In general, PSI is known to be much more stable, also at high temperatures, than PSII (Berry and Bjö rkman, 1980;Takeuchi and Thornber, 1994;Al-Khatib and Paulsen, 1999), but in the CL3 mutant PSI was more affected than PSII. The biochemical, spectroscopic, and physiological phenotype resembles that described for several other PSI mutants, where the amount of PSI is decreased and a secondary damage to PSII and other thylakoid proteins is observed especially at higher light intensity and with light that predominantly excites PSII (Haldrup et al, 2000(Haldrup et al, , 2003.…”
Section: Discussionmentioning
confidence: 64%
“…Likewise, changes in core complex subunits of PSI were relatively weak with PsaD and PsaK upregulated two-to threefold. Beyond sustaining PSI function, the role of PsaD is unclear (Haldrup et al, 2003); however, PsaK appears to interact with LHCI and may stabilize the association of LHCI with the PSI core complex (Jensen et al, 2000). The lumenal electron carrier plastocyanin was also stimulated by GLK1 expression, perhaps reflecting the increased electron flow associated with enhanced light interception by LHC antennae.…”
Section: Light-harvesting Antenna Proteins Are Significantly Upregulamentioning
confidence: 89%
“…Six of the PSI core proteins (PsaD, PsaE, and PsaH) are found in pairs of closely related paralogues. Functional analysis has been performed for several of them (Varotto et al, 2000(Varotto et al, , 2002Scheller et al, 2001;Haldrup et al, 2003). Despite the very high level of sequence identity between psaE1 and psaE2 and between psaH1 and psaH2 (89 and 99%, respectively), we found unique sequence tags (by ESI-MS/MS) for each and a unique (diagnostic) tag for psaD-2 (98% sequence identity with psaD-1) in the pepsin digest of fraction C/M 1:1 RP-HPLC.…”
Section: Thylakoid Photosynthetic Apparatusmentioning
confidence: 99%