Pigment Binding, Fluorescence Properties, and Oligomerization Behavior of Lhca5, a Novel Light-harvesting Protein

Storf, Stefanie; Jansson, Stefan; Schmid, Volkmar

doi:10.1074/jbc.m411248200

Cited by 34 publications

(27 citation statements)

References 45 publications

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“…These particles comprise Lhca1, Lhca2, Lhca3, and Lhca5, most likely as Lhca1/5 and Lhca2/3 dimers. This is supported by a mass spectrometry study where Lhca5 was detected in the LHCI-730 fraction, suggesting an interaction with Lhca1 or Lhca4 (14) and by the in vitro reconstitution results, which showed that the Lhca1/5 dimer can be obtained (13). This novel PSI-Lhca1/5-Lhca2/3 complex is as stable as the WT complex, indicating that Lhca5 is a perfect substitute for Lhca4 in the assembly of the system.…”

Section: Lhca1 -2 -3 and -4 Have A Fixed Position In The Psi Strucmentioning

confidence: 53%

“…Its expression level is higher in mutant plants depleted in Lhca1 and Lhca4; however no corresponding polypeptide could be detected on SDS-PAGE, indicating that even in these mutants, Lhca5 is not present in stoichiometric amounts with the core (11). Based on cross-linking studies, Lhca5 has been suggested to form homodimers (12), but in vitro reconstitution has shown that it can form heterodimers with Lhca1 (13,14).…”

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confidence: 99%

“…It was shown that Asn as a ligand for Chl A5 is required for the strong red-shifted absorption and emission of Lhca3 and Lhca4 (18). In Lhca5 the ligand for Chl A5 is a His, as in Lhca1 and Lhca2, and accordingly it does not contain low-energy Chls (13).…”

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confidence: 99%

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The Role of Lhca Complexes in the Supramolecular Organization of Higher Plant Photosystem I

Wientjes

Oostergetel

Jansson

et al. 2009

Journal of Biological Chemistry

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In this work, Photosystem I supercomplexes have been purified from Lhca-deficient lines of Arabidopsis thaliana using a mild detergent treatment that does not induce loss of outer antennas. The complexes have been studied by integrating biochemical analysis with electron microscopy. This allows the direct correlation of changes in protein content with changes in supramolecular structure of Photosystem I to get information about the position of the individual Lhca subunits, the association of the antenna to the core, and the influence of the individual subunits on the stability of the system. Photosystem I complexes with only two or three antenna complexes were purified, showing that the binding of Lhca1/4 and Lhca2/3 dimers to the core is not interdependent, although weak binding of Lhca2/3 to the core is stabilized by the presence of Lhca4. Moreover, Lhca2 and Lhca4 can be associated with the core in the absence of their "dimeric partners." The structure of Photosystem I is very rigid, and the absence of one antenna complex leaves a "hole" in the structure that cannot be filled by other Lhcas, clearly indicating that the docking sites for the individual subunits are highly specific. There is, however, an exception to the rule: Lhca5 can substitute for Lhca4, yielding highly stable PSI supercomplexes with a supramolecular organization identical to the WT.

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Section: Lhca1 -2 -3 and -4 Have A Fixed Position In The Psi Strucmentioning

confidence: 53%

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confidence: 99%

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The Role of Lhca Complexes in the Supramolecular Organization of Higher Plant Photosystem I

Wientjes

Oostergetel

Jansson

et al. 2009

Journal of Biological Chemistry

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“…When expressed sequence tag (EST) data from Arabidopsis (Arabidopsis thaliana) started to accumulate, the Lhc genes of Arabidopsis were subjected to detailed characterization, and three additional types of genes (denoted as Lhca5, Lhca6, and Lhcb4.3) that appeared to be expressed at very low levels or not at all were identified (Jansson, 1999). These genes (referred to as rarely expressed in the following) have started to gain some attention, but the corresponding proteins have not yet been well characterized, except Lhca5 (Ganeteg et al, 2004;Storf et al, 2004Storf et al, , 2005. The Lhc supergene family of higher plants also contains genes coding for proteins that exhibit sequence similarity to the Lhc proteins, namely, the four-helix protein PsbS and the light-harvesting-like (LIL) proteins.…”

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Abundantly and Rarely Expressed Lhc Protein Genes Exhibit Distinct Regulation Patterns in Plants

et al. 2006

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We have analyzed gene regulation of the Lhc supergene family in poplar (Populus spp.) and Arabidopsis (Arabidopsis thaliana) using digital expression profiling. Multivariate analysis of the tissue-specific, environmental, and developmental Lhc expression patterns in Arabidopsis and poplar was employed to characterize four rarely expressed Lhc genes, Lhca5, Lhca6, Lhcb7, and Lhcb4.3. Those genes have high expression levels under different conditions and in different tissues than the abundantly expressed Lhca1 to 4 and Lhcb1 to 6 genes that code for the 10 major types of higher plant light-harvesting proteins. However, in some of the datasets analyzed, the Lhcb4 and Lhcb6 genes as well as an Arabidopsis gene not present in poplar (Lhcb2.3) exhibited minor differences to the main cooperative Lhc gene expression pattern. The pattern of the rarely expressed Lhc genes was always found to be more similar to that of PsbS and the various light-harvesting-like genes, which might indicate distinct physiological functions for the rarely and abundantly expressed Lhc proteins. The previously undetected Lhcb7 gene encodes a novel plant Lhcb-type protein that possibly contains an additional, fourth, transmembrane N-terminal helix with a highly conserved motif. As the Lhcb4.3 gene seems to be present only in Eurosid species and as its regulation pattern varies significantly from that of Lhcb4.1 and Lhcb4.2, we conclude it to encode a distinct Lhc protein type, Lhcb8.

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“…Lhca6 has not been localized so far but for Lhca5 an association with PSI-LHCI has been demonstrated in Arabidopsis and tomato [13,14]. Studies of Lhca5 reconstituted in vitro have revealed a pigment-binding pattern typical for Lhca proteins and indicated heterodimer formation with Lhca1 [15]. Comparisons of Arabidopsis lines lacking Lhca5 with the wildtype (wt) indicated that Lhca5 is present only in substoichiometrical amounts and might not play a major role for higher plant light-harvesting, at least under standard conditions [13].…”

Section: Introductionmentioning

confidence: 99%

Lhca5 interaction with plant photosystem I

Luciński¹,

Schmid²,

Jansson³

et al. 2006

FEBS Letters

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In the outer antenna (LHCI) of higher plant photosystem I (PSI) four abundantly expressed light-harvesting protein of photosystem I (Lhca)-type proteins are organized in two heterodimeric domains (Lhca1/Lhca4 and Lhca2/Lhca3). Our cross-linking studies on PSI-LHCI preparations from wildtype Arabidopsis and pea plants indicate an exclusive interaction of the rarely expressed Lhca5 light-harvesting protein with LHCI in the Lhca2/Lhca3-site. In PSI particles with an altered LHCI composition Lhca5 assembles in the Lhca1/Lhca4 site, partly as a homodimer. This flexibility indicates a binding-competitive model for the LHCI assembly in plants regulated by molecular interactions of the Lhca proteins with the PSI core.

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Pigment Binding, Fluorescence Properties, and Oligomerization Behavior of Lhca5, a Novel Light-harvesting Protein

Cited by 34 publications

References 45 publications

The Role of Lhca Complexes in the Supramolecular Organization of Higher Plant Photosystem I

The Role of Lhca Complexes in the Supramolecular Organization of Higher Plant Photosystem I

Abundantly and Rarely Expressed Lhc Protein Genes Exhibit Distinct Regulation Patterns in Plants

Lhca5 interaction with plant photosystem I

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