Crystal structure of CyanoQ from the thermophilic cyanobacterium Thermosynechococcus elongatus and detection in isolated photosystem II complexes

Michoux, Franck; Boehm, Marko; Białek, Wojciech; Takasaka, K.; Maghlaoui, Karim; Barber, James; Murray, James W.; Nixon, Peter J.

doi:10.1007/s11120-014-0010-z

Cited by 27 publications

(20 citation statements)

References 54 publications

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“…This is known to occur during isolation and crystallization of cyanobacterial PS II. The CyanoQ component is lost [17,162] and does not appear in the current crystal structures [6,7]. Possible reasons for the loss of subunits include release at the detergent concentrations used during solubilization of the photosynthetic membrane, loss during purification, the ionic make-up of the crystallization liquor (usually very different fromin vivo conditions), sensitivity to required crystallization conditions (pH, metal additives, amphiphilic additives, etc.…”

Section: 32in Vivoand In Organelloprotein Crosslinkingmentioning

confidence: 97%

“…These proteins, CyanoP and CyanoQ, however are not present in any cyanobacterial crystal structure available. While the constitutive association of CyanoP with cyanobacterial PS II and its function is controversial [159][160][161], CyanoQ is a constitutive subunit of cyanobacterial PS II [162] which is lost during crystallization [161]. CyanoQ may also serve as an assembly factor, as multiple copies of CyanoQ are present in a late cyanobacterial PS II assembly complex [163].…”

Section: Location Of Cyanoq Within Cyanobacterial Ps IImentioning

confidence: 99%

“…Additionally X-ray crystallography and multidimensional nuclear magnetic resonance studieshave provided structures for a variety of isolated extrinsic protein subunits of photosynthetic complexes not presentin the current crystal structures of PS II. These include CyanoQ, PsbQ [17][18][19][20], CyanoP and PsbP [21][22][23][24].…”

Section: Introductionmentioning

confidence: 99%

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Recent advances in the use of mass spectrometry to examine structure/function relationships in photosystem II

Bricker

Mummadisetti

Frankel

2015

Journal of Photochemistry and Photobiology B: Biology

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Tandem mass spectrometry often coupled with chemical modification techniques, is developing into increasingly important tool in structural biology. These methods can provide important supplementary information concerning the structural organization and subunit make-up of membrane protein complexes, identification of conformational changes occurring during enzymatic reactions, identification of the location of posttranslational modifications, and elucidation of the structure of assembly and repair complexes. In this review, we will present a brief introduction to Photosystem II, tandem mass spectrometry and protein modification techniques that have been used to examine the photosystem. We will then discuss a number of recent case studies that have used these techniques to address open questions concerning PS II. These include the nature of subunit-subunit interactions within the phycobilisome, the interaction of phycobilisomes with Photosystem I and the Orange Carotenoid Protein, the location of CyanoQ, PsbQ and PsbP within Photosystem II, and the identification of phosphorylation and oxidative modification sites within the photosystem. Finally, we will discuss some of the future prospects for the use of these methods in examining other open questions in PS II structural biochemistry.

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Section: 32in Vivoand In Organelloprotein Crosslinkingmentioning

confidence: 97%

Section: Location Of Cyanoq Within Cyanobacterial Ps IImentioning

confidence: 99%

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Recent advances in the use of mass spectrometry to examine structure/function relationships in photosystem II

Bricker

Mummadisetti

Frankel

2015

Journal of Photochemistry and Photobiology B: Biology

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“…Psb27 is then replaced by these proteins upon assembly of the Mn cluster (Roose and Pakrasi 2008). Psb27 has been reported to occur in sub-stochiometric amounts compared to other PSII subunits in T. elongatus (Michoux et al 2014). If this is also the case in Prochlorococcus strains lacking PsbU and PsbV, this would plead against a role of Psb27 in shielding of the Mn cluster.…”

Section: Discussionmentioning

confidence: 99%

Comparison of photosynthetic performances of marine picocyanobacteria with different configurations of the oxygen-evolving complex

et al. 2018

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The extrinsic PsbU and PsbV proteins are known to play a critical role in stabilizing the MnCaO cluster of the PSII oxygen-evolving complex (OEC). However, most isolates of the marine cyanobacterium Prochlorococcus naturally miss these proteins, even though they have kept the main OEC protein, PsbO. A structural homology model of the PSII of such a natural deletion mutant strain (P. marinus MED4) did not reveal any obvious compensation mechanism for this lack. To assess the physiological consequences of this unusual OEC, we compared oxygen evolution between Prochlorococcus strains missing psbU and psbV (PCC 9511 and SS120) and two marine strains possessing these genes (Prochlorococcus sp. MIT9313 and Synechococcus sp. WH7803). While the low light-adapted strain SS120 exhibited the lowest maximal O evolution rates (P per divinyl-chlorophyll a, per cell or per photosystem II) of all four strains, the high light-adapted strain PCC 9511 displayed even higher P and P at high irradiance than Synechococcus sp. WH7803. Furthermore, thermoluminescence glow curves did not show any alteration in the B-band shape or peak position that could be related to the lack of these extrinsic proteins. This suggests an efficient functional adaptation of the OEC in these natural deletion mutants, in which PsbO alone is seemingly sufficient to ensure proper oxygen evolution. Our study also showed that Prochlorococcus strains exhibit negative net O evolution rates at the low irradiances encountered in minimum oxygen zones, possibly explaining the very low O concentrations measured in these environments, where Prochlorococcus is the dominant oxyphototroph.

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“…21,69 Recently, CyanoQ was also found in purified PSII core complexes from T. elongatus. 22 In contrast, CyanoP may not be stoichiometrically involved in PSII complexes 20,22 and was suggested to function during the assembly and/or photoactivation process of PSII. 70 On the other hand, neither CyanoP nor CyanoQ has been found in the crystal structures of PSII core complexes from T. elongatus 7,8 and T. vlucanus.…”

Section: ■ Discussionmentioning

confidence: 99%

Effects of Extrinsic Proteins on the Protein Conformation of the Oxygen-Evolving Center in Cyanobacterial Photosystem II As Revealed by Fourier Transform Infrared Spectroscopy

2015

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Extrinsic proteins of photosystem II (PSII) play an important role in optimizing oxygen-evolving reactions in all oxyphototrophs. The currently available crystal structures of cyanobacterial PSII core complexes show the binding structures of the extrinsic proteins, PsbO, PsbV, and PsbU; however, how the individual extrinsic proteins affect the structure and the function of the oxygen-evolving center (OEC) in cyanobacterial PSII remains unknown. In this study, we have investigated the effects of the binding of the extrinsic proteins on the protein conformation of the OEC in PSII core complexes from the thermophilic cyanobacterium Thermosynechococcus elongatus, using light-induced Fourier transform infrared (FTIR) difference spectroscopy. Upon removal of the three extrinsic proteins, an S₂-minus-S₁ FTIR difference spectrum measured in the presence of a high CaCl₂ concentration showed a drastic change in amide I bands, reflecting perturbation of the secondary structures of polypeptides, whereas the overall spectral intensity was lost at a low CaCl₂ concentration, indicative of inactivation of the Mn₄CaO₅ cluster. The amide I features as well as the overall intensity were recovered mainly by binding of PsbO, while complete amide I recovery was achieved by further binding of PsbV and PsbU. We thus concluded that PsbO, together with smaller contributions of PsbV and PsbU, plays a role in the maintenance of the proper protein conformation of the OEC in cyanobacterial PSII, which provides the stability of the Mn₄CaO₅ cluster via the enhanced retention capability of Ca²⁺ and Cl⁻ ions.

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Crystal structure of CyanoQ from the thermophilic cyanobacterium Thermosynechococcus elongatus and detection in isolated photosystem II complexes

Cited by 27 publications

References 54 publications

Recent advances in the use of mass spectrometry to examine structure/function relationships in photosystem II

Recent advances in the use of mass spectrometry to examine structure/function relationships in photosystem II

Comparison of photosynthetic performances of marine picocyanobacteria with different configurations of the oxygen-evolving complex

Effects of Extrinsic Proteins on the Protein Conformation of the Oxygen-Evolving Center in Cyanobacterial Photosystem II As Revealed by Fourier Transform Infrared Spectroscopy

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