Direct evidence for cooperation of the 17‐ and 23‐kDa proteins in the recovery of oxygen evolution in cholate‐treated thylakoids

Fukutaka, Eitaro; Imaoka, Akiko; Akabori, Kozo; Toyoshima, Yoshinori

doi:10.1016/0014-5793(83)80581-x

Cited by 23 publications

(6 citation statements)

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“…In an early mutant study on Chlamydomonas it was shown that a mutant devoid of oxygen-evolving capacity lacked 3 extrinsic proteins of 21-, 18-, and 6-kDa [18]. Authors in [3] showed that the restoration of oxygen evolution with their 24-and 17-kDa proteins in cholate-NaCl-extracted thylakoids could be enhanced by an unknown component of less than 15 kDa. Inactivation of oxygen evolution by treatment of thylakoids with lauroyl choline chloride released among several polypeptides one at 10 kDa [19].…”

Section: Resultsmentioning

confidence: 99%

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The release of a 10‐kDa polypeptide from everted photosystem II thylakoid membranes by alkaline tris

1984

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The release of polypeptides from inside-out thylakoid vesicles and photosystem II by alkaline Tris treatment was reinvestigated, using SDS-polyacrylamide gel electrophoresis (PAGE) in the presence of urea, with highly increased resolution in the low molecular mass region. In addition to the 33-, 23-, and 1bkDa proteins of the oxygen-evolving complex, a IO-kDa polypeptide was released. This IO-kDa polypeptide is an entrinsic polypeptide located at the inner grana thylakoid surface and with a likely role in photosynthetic oxygen evolution.

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Section: Resultsmentioning

confidence: 99%

“…[l]). Partial restoration of the lost activity in the treated photosystem II preparations has been obtained with each of the 3 proteins [2][3][4][5]. At present, most data suggest that these proteins are involved in mediating the calcium and/or chloride necessary for optimal oxygen evolution [6-lo].…”

Section: Introductionmentioning

confidence: 99%

The release of a 10‐kDa polypeptide from everted photosystem II thylakoid membranes by alkaline tris

1984

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“…Inactivation of oxygen evolution by treatment of thylakoids with dodecyl choline chloride released, among several polypeptides, one of 10-kDa molecular mass [36]. Fukutaka et al [37] reported that restoration of oxygen evolution with the 23-kDa and 16-kDa proteins in NaCl/cholate-treated thylakoids could be enhanced by an unknown component of less than 15 kDa. The 10-kDa polypeptide isolated in the present study was also partly released by a similar NaCl/cholate treatment.…”

Section: Relation Of the 22-kda And 10-kda Polypeptides To Other Polymentioning

confidence: 99%

Isolation and characterization of the 10‐kDa and 22‐kDa polypeptides of higher plant photosystem 2

Ljungberg

Åkerlund

Andersson

1986

European Journal of Biochemistry

132

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Two polypeptides of 10 kDa and 22 kDa, shown to be components of the higher plant photosystem 2, were purified and examined. A NaCl/Triton X-100 treatment was designed, which released these two polypeptides from the thylakoid membrane, in concert with the extrinsic 16-kDa and 23-kDa proteins, concomitant with a loss in oxygen-evolution activity. After this treatment the oxygen-evolving activity of the photosystem 2 membranes devoid of the 10-kDa and the 22-kDa polypeptides could be restored with CaC12, but not by readdition of the purified 23-kDa protein. This defiency was caused by an inability of the 23-kDa protein to rebind to the photosystem 2 membranes. In analogy, the oxygen-evolution activity of a highly purified photosystem 2 core preparation, devoid of the 10-kDa and 22-kDa polypeptides, was stimulated by CaC12, but not by the 23-kDa protein. We, therefore, suggest that the 1 0-kDa or the 22-kDa polypeptides provide a binding-site for the extrinsic 23-kDa protein to the thylakoid membrane.The 1 0-kDa and 22-kDa polypeptides were isolated through ion-exchange chromatography in the presence of detergents. They both displayed hydrophobic properties, verified by their low proportion of polar amino acid residues and their partition to the hydrophobic phase during Triton X-114 fractionation. The purified polypeptides did not contain metallic cofactors or substances with absorption in the visible region of the spectrum.In recent years extensive knowledge about biophysics, biochemistry and molecular biology of higher plant photosystem 2 has accumulated (reviewed in [l -31). The present concept of the photosystem 2 is of a supramolecular complex, with both integral and peripheral protein subunits, mainly located in the grana region of the thylakoid membrane. A number of studies have indicated that the catalytic photosystem 2 core complex is made up of at least five different hydrophobic proteins [4 -61 and a number of low-molecular-mass polypeptides [7]. In addition extrinsic proteins of 33 kDa, 23 kDa and 16 kDa have been shown to be located at the inner thylakoid surface and to be regulatory components of the oxygen-evolving complex of photosystem 2. The 33-kDa protein seems to have a stabilizing effect on the catalytic manganese, while the 23-kDa and the 16-kDa proteins are involved in the binding of the calcium and chloride necessary for oxygen evolution [2].In an immunoprecipitation study we have previously shown that a close structural association exists between the 33-kDa and 23-kDa proteins, and three polypeptides of 10 kDa, 22 kDa and 24 kDa [8]. Furthermore, the 10-kDa polypeptide was found to be released from everted photosystem 2 membranes by alkaline Tris [9], a treatment which inhibits oxygen evolution. A nearest-neighbor analysis, using chemical cross-linking, also revealed a close proximity between the 33-kDa protein and 22-kDa and 24-kDa polypeptides [lo].In the present study we report the isolation and chardcterization of the two polypeptides of 10 kDa and 22 kDa. MATERIALS AND METHODS Sub-thy...

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“…In [8] it was reported that the inhibition of the 02 evolution in inside-out thylakoid was proportional to the amount of released 23-kDa protein, while authors in [3] showed the recovery of the 02 evolution by simultaneous reinsertion of the 17-and 23-kDa proteins in cholate-treated thylakoids but not each protein alone. Authors in [lo] claimed that for the PS II particles from which the 17-and 23-kDa proteins were completely depleted by NaCl washing, the activity remained at about 40% of the original level.…”

Section: Abbreviationsmentioning

confidence: 99%

Reconstitution of photosynthetic charge accumulation and oxygen evolution in CaCl₂‐treated PS II particles

et al. 1984

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The reconstitution of high 0, evolution in CaCl,-treated PS II particles was achieved by the simultaneous addition of the 17-, 23-and 34kDa proteins and total thylakoid lipids in the presence of 25% glycerol and 15 mM sodium cholate. The activity of the reconstituted membranes recovered to 85% of that of the nondepleted original PS II particles at the optimal condition. By means of this reconstitution method, evidence for the cooperation of the three proteins in the recovery of 0, evolution in the CaCl,-treated PS II particles was found by changing the concentration of NaCl in the assay medium, and the relationship between the amount of manganese retained in the water-splitting complex and the 0, evolving activity was examined by using the partially solubilized PS II particles with n-octyl-/I-D-glucoside.

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Direct evidence for cooperation of the 17‐ and 23‐kDa proteins in the recovery of oxygen evolution in cholate‐treated thylakoids

Cited by 23 publications

References 5 publications

The release of a 10‐kDa polypeptide from everted photosystem II thylakoid membranes by alkaline tris

The release of a 10‐kDa polypeptide from everted photosystem II thylakoid membranes by alkaline tris

Isolation and characterization of the 10‐kDa and 22‐kDa polypeptides of higher plant photosystem 2

Reconstitution of photosynthetic charge accumulation and oxygen evolution in CaCl₂‐treated PS II particles

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Direct evidence for cooperation of the 17‐ and 23‐kDa proteins in the recovery of oxygen evolution in cholate‐treated thylakoids

Cited by 23 publications

References 5 publications

The release of a 10‐kDa polypeptide from everted photosystem II thylakoid membranes by alkaline tris

The release of a 10‐kDa polypeptide from everted photosystem II thylakoid membranes by alkaline tris

Isolation and characterization of the 10‐kDa and 22‐kDa polypeptides of higher plant photosystem 2

Reconstitution of photosynthetic charge accumulation and oxygen evolution in CaCl2‐treated PS II particles

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Reconstitution of photosynthetic charge accumulation and oxygen evolution in CaCl₂‐treated PS II particles