Secondary structure and thermostability of the photosystem II manganese-stabilizing protein of the thermophilic cyanobacterium Synechococcus elongatus

Sonoyama, Masashi; Motoki, Akihiro; Okamoto, Genichi; Hirano, Masahiko; Ishida, Hideyuki; Katoh, Sakae

doi:10.1016/s0167-4838(96)00099-4

Cited by 24 publications

(30 citation statements)

References 22 publications

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“…The wild-type protein contains ␤-sheet severalfold more abundantly than ␣-helix. The values are similar to those of spinach MSP (42-44) but different from the previous estimate from the CD spectrum in the 197-250 nm region, which predicted a higher proportion of ␣-helix and a lower proportion of ␤-sheet than those shown in Table III (41). Although not shown here, Fourier-transform infrared spectroscopy with an improved precision also indicated a larger abundance of ␤-sheets than shown previously (41). The mutations that significantly decreased the binding and reactivating abilities of MSP had no significant effect on the secondary conformation of the protein; small variations in the proportion of the secondary structure elements observed are in the range of experimental error.…”

Section: Binding Of Msp To Photosystem II 14750supporting

confidence: 47%

“…The secondary conformation of the protein has previously been estimated from the UV CD spectrum in the 197-250 nm region as well as Fourier-transform infrared spectrum (41). Because CD data provide more accurate estimates of the proportions of secondary structure elements when the CD spectrum is extended to shorter wavelengths (35), the CD spectra of wild-type and mutant proteins were determined from 181 to 260 nm.…”

Section: Binding Of Msp To Photosystem II 14750mentioning

confidence: 99%

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

Motoki¹,

Usui²,

Shimazu³

et al. 2002

Journal of Biological Chemistry

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Section: Binding Of Msp To Photosystem II 14750supporting

confidence: 47%

Section: Binding Of Msp To Photosystem II 14750mentioning

confidence: 99%

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

Motoki¹,

Usui²,

Shimazu³

et al. 2002

Journal of Biological Chemistry

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“…Both S-MSP and T-MSP are thermostable, and have unfolding transitions which exhibit low cooperativity which is consistent with their assignment as molten globular proteins (Heredia and De Las Rivas 2003;Loll et al 2005a;Lydakis-Simantiris et al 1999;Sonoyama et al 1996). Both can refold after heating to 90°C and can restore activity to PSII upon cooling to 25°C (LydakisSimantiris et al 1999;Sonoyama et al 1996).…”

Section: Thermostability Of Mspmentioning

confidence: 55%

“…But PSII reconstituted with a T-MSP-thioredoxin fusion protein that had lower thermal stability than the T-MSP had a lower Ca 2? requirement for T. elongatus CD 19 24 57 Sonoyama et al (1996) T. elongatus CD 8 43 48 Loll et al (2005a) T. elongatus FTIR 23.6 32.5 43.9 Loll et al (2005a) maximum activity, suggesting that Ca 2? may increase PSII activity by modulating the flexibility of the MSP (Williamson et al 2007).…”

Section: The Effect Of Metal Ions and Ph On Msp Structurementioning

confidence: 99%

Structural and functional aspects of the MSP (PsbO) and study of its differences in thermophilic versus mesophilic organisms

Williamson

2008

Photosynth Res

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The Manganese Stabilizing Protein (MSP) of Photosystem II (PSII) is a so-called extrinsic subunit, which reversibly associates with the other membrane-bound PSII subunits. The MSP is essential for maximum rates of O(2) production under physiological conditions as stabilizes the catalytic [Mn(4)Ca] cluster, which is the site of water oxidation. The function of the MSP subunit in the PSII complex has been extensively studied in higher plants, and the structure of non-PSII associated MSP has been studied by low-resolution biophysical techniques. Recently, crystal structures of PSII from the thermophilic cyanobacterium Thermosynechococcus elongatus have resolved the MSP subunit in its PSII-associated state. However, neither any crystal structure is available yet for MSP from mesophilic organisms, higher plants or algae nor has the non-PSII associated form of MSP been crystallized. This article reviews the current understanding of the structure, dynamics, and function of MSP, with a particular focus on properties of the MSP from T. elongatus that may be attributable to the thermophilic ecology of this organism rather than being general features of MSP.

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“…"Synechococcus elongatus," which has been maintained in Toray Research Center, Inc., Japan, is located near the root of the NJ and ML trees with Gloeobacter violaceus strain PCC 7421. This thermophilic strain, collected from a hot spring in Beppu, Kyushu, Japan, was well grown at 55°C (Yamaoka et al 1978) and has been examined by physiological approaches (e.g., Sonoyama et al 1996). On the other hand, Rippka and CohenBazire (1983) proposed the PCC 6301 strain as the type of strain of Synechococcus elongatus.…”

Section: Discussionmentioning

confidence: 99%

Detection of Seven Major Evolutionary Lineages in Cyanobacteria Based on the 16S rRNA Gene Sequence Analysis with New Sequences of Five Marine Synechococcus Strains

1999

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Although molecular phylogenetic studies of cyanobacteria on the basis of the 16S rRNA gene sequence have been reported, the topologies were unstable, especially in the inner branchings. Our analysis of 16S rRNA gene phylogeny by the maximum-likelihood and neighbor-joining methods combined with rate homogeneous and heterogeneous models revealed seven major evolutionary lineages of the cyanobacteria, including prochlorophycean organisms. These seven lineages are always stable on any combination of these methods and models, fundamentally corresponding to phylogenetic relationships based on other genes, e.g., psbA, rbcL, rnpB, rpoC, and tufA. Moreover, although known genotypic and phenotypic characters sometimes appear paralleled in independent lineages, many characters are not contradictory within each group. Therefore we propose seven evolutionary groups as a working hypothesis for successive taxonomic reconstruction. New 16S rRNA sequences of five unicellular cyanobacterial strains, PCC 7001, PCC 7003, PCC 73109, PCC 7117, and PCC 7335 of Synechococcus sp., were determined in this study. Although all these strains have been assigned to "marine clusters B and C," they were separated into three lineages. This suggests that the organisms classified in the genus Synechococcus evolved diversely and should be reclassified in several independent taxonomic units. Moreover, Synechococcus strains and filamentous cyanobacteria make a monophyletic group supported by a comparatively high statistical confidence value (80 to 100%) in each of the two independent lineages; therefore, these monophylies probably reflect the convergent evolution of a multicellular organization.

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Secondary structure and thermostability of the photosystem II manganese-stabilizing protein of the thermophilic cyanobacterium Synechococcus elongatus

Cited by 24 publications

References 22 publications

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

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

Structural and functional aspects of the MSP (PsbO) and study of its differences in thermophilic versus mesophilic organisms

Detection of Seven Major Evolutionary Lineages in Cyanobacteria Based on the 16S rRNA Gene Sequence Analysis with New Sequences of Five Marine Synechococcus Strains

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