A Domain of the Manganese-stabilizing Protein fromSynechococcus elongatus Involved in Functional Binding to Photosystem II

Motoki, Akihiro; Usui, Mina; Shimazu, Tsuneo; Hirano, Masahiko; Katoh, Sakae

doi:10.1074/jbc.m100766200

Cited by 30 publications

(38 citation statements)

References 42 publications

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“…However, this alignment requires insertion of a gap (dashes) in the cyanobacterial sequence. This agrees with other published strategies for aligning MSP sequences from eukaryotes and cyanobacteria, which require introductions of gaps in sequences from one set of species or the other (3,46,49). This gap is probably a consequence of the absence of one of the binding recognition sequences in the cyanobacterial protein.…”

Section: Discussionsupporting

confidence: 89%

“…Only one study of MSP stoichiometries required for reconstitution in cyanobacteria is currently available (46), and in that investigation it is not entirely clear that binding of one copy of recombinant protein is sufficient to saturate PSII binding sites. From the results of Table 2, it is nevertheless apparent that cyanobacteria lack one of the sequences that is essential for binding of two copies of eukaryotic MSP to PSII.…”

Section: Discussionmentioning

confidence: 99%

“…From the results of Table 2, it is nevertheless apparent that cyanobacteria lack one of the sequences that is essential for binding of two copies of eukaryotic MSP to PSII. This conclusion is also apparent in the sequence alignments in ref 49. An alternate alignment of these sequences is possible (3,46):…”

Section: Discussionmentioning

confidence: 99%

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N-Terminal Truncations of Manganese Stabilizing Protein Identify Two Amino Acid Sequences Required for Binding of the Eukaryotic Protein to Photosystem II and Reveal the Absence of One Binding-Related Sequence in Cyanobacteria

Popelková

Yocum

2002

Biochemistry

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Manganese stabilizing protein (MSP) is an intrinsically disordered extrinsic subunit of photosystem II that regulates the stability and kinetic performance of the tetranuclear manganese cluster that oxidizes water to oxygen. An earlier study showed that deletion of the (1)E-(3)G domain of MSP caused no loss of activity reconstitution, whereas deletion of the (4)K-(10)E domain reduced binding of the protein from 2 to 1 mol of MSP/mol of photosystem II and lowered activity reconstitution to about 50% of the control value [Popelkova et al. (2002) Biochemistry 41, 2702-2711]. In this work we present evidence that deletion of 13 or 14 amino acid residues from the MSP N-terminus (mutants DeltaS13M and DeltaK14M) does not interfere either with functional binding of one copy of MSP to photosystem II or with reconstitution of oxygen evolution activity to 50% of the control level. Both of these mutants exhibit nonspecific binding to photosystem II at higher protein concentrations. Truncation of the MSP sequence by 18 amino acids (mutant DeltaE18M), however, causes a loss of protein binding and activity reconstitution. This result demonstrates that the N-terminal domain (15)T-(18)E is required for binding of at least one copy of MSP to photosystem II. Analyses of CD spectra reveal changes in the structure of DeltaE18M (loss of beta-sheet, gain of unordered structure). Use of the information gained from these experiments in analyses of N-terminal sequences of MSP from a number of species indicates that higher plants and algae possess two recognition domains that are required for MSP binding to PSII, whereas cyanobacteria lack the first N-terminal domain found in eukaryotes. This may explain the absence of a second copy of MSP in the crystal structure of PSII from Synechococcus elongatus [Zouni et al. (2001) Nature 409, 739-743].

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Section: Discussionsupporting

confidence: 89%

Section: Discussionmentioning

confidence: 99%

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N-Terminal Truncations of Manganese Stabilizing Protein Identify Two Amino Acid Sequences Required for Binding of the Eukaryotic Protein to Photosystem II and Reveal the Absence of One Binding-Related Sequence in Cyanobacteria

Popelková

Yocum

2002

Biochemistry

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“…5a. In the cyanobacterial PsbO, Motoki et al (2002) showed that substitution of R152, D158, K160, or R162 with uncharged residues significantly decreased its binding ability and implied that the V148-G163 sequence which exists in domain IV of Fig. 5a is a domain for functional interaction with PSII.…”

Section: Structure and Function Of Psbomentioning

confidence: 98%

Structures and functions of the extrinsic proteins of photosystem II from different species

et al. 2008

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This minireview presents a summary of information available on the variety and binding properties of extrinsic proteins that form the oxygen-evolving complex of photosystem II (PSII) of cyanobacteria, red alga, diatom, green alga, euglena, and higher plants. In addition, the structure and function of extrinsic PsbO, PsbV, and PsbU proteins are summarized based on the crystal structure of thermophilic cyanobacterial PSII together with biochemical and genetic studies from various organisms.

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“…A number of studies have shown that the primary amino acid sequences of MSPs from various photosynthetic organisms are homologous ( , ). One of the most conserved domains is the region Phe145−Gly163 (spinach numbering) that includes two fully conserved arginyl residues (R151 and R161) in all known MSP sequences.…”

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confidence: 99%

Mutagenesis of Basic Residues R151 and R161 in Manganese-Stabilizing Protein of Photosystem II Causes Inefficient Binding of Chloride to the Oxygen-Evolving Complex

et al. 2006

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Manganese-stabilizing protein of photosystem II, an intrinsically disordered polypeptide, contains a high ratio of charged to hydrophobic amino acid residues. Arg151 and Arg161 are conserved in all known MSP sequences. To examine the role of these basic residues in MSP structure and function, three mutants of spinach MSP, R151G, R151D, and R161G, were produced. Here, we present evidence that replacement of Arg151 or Arg161 yields proteins that have lower PSII binding affinity, and are functionally deficient even though about 2 mol of mutant MSP/mol PSII can be rebound to MSP depleted PSII membranes. R161G reconstitutes O(2) evolution activity to 40% of the control, while R151G and R151D reconstitute only 20% of the control activity. Spectroscopic and biochemical techniques fail to detect significant changes in solution structure. More extensive O(2) evolution assays revealed that the Mn cluster is stable in samples reconstituted with each mutated MSP, and that all three Arg mutants have the same ability to retain Ca(2+) as the wild-type protein. Activity assays exploring the effect of these mutations on retention of Cl(-), however, showed that the R151G, R151D, and R161G MSPs are defective in Cl(-) binding to the OEC. The mutants have Cl(-) K(M) values that are about four (R161G) or six times (R151G and R151D) higher than the value for the wild-type protein. The results reported here suggest that conserved positive charges on the manganese-stabilizing protein play a role in proper functional assembly of the protein into PSII, and, consequently, in retention of Cl(-) by the O(2)-evolving complex.

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A Domain of the Manganese-stabilizing Protein fromSynechococcus elongatus Involved in Functional Binding to Photosystem II

Cited by 30 publications

References 42 publications

N-Terminal Truncations of Manganese Stabilizing Protein Identify Two Amino Acid Sequences Required for Binding of the Eukaryotic Protein to Photosystem II and Reveal the Absence of One Binding-Related Sequence in Cyanobacteria

N-Terminal Truncations of Manganese Stabilizing Protein Identify Two Amino Acid Sequences Required for Binding of the Eukaryotic Protein to Photosystem II and Reveal the Absence of One Binding-Related Sequence in Cyanobacteria

Structures and functions of the extrinsic proteins of photosystem II from different species

Mutagenesis of Basic Residues R151 and R161 in Manganese-Stabilizing Protein of Photosystem II Causes Inefficient Binding of Chloride to the Oxygen-Evolving Complex

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