Mastigocladus laminosus

Whitelegge, J.P, Zhang, H., Aguilera, R., Taylor, R.M., Cramer, W.A. (2002). Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein cytochrome b(6)f complex from spinach and the cyanobacterium Mastigocladus laminosus. Mol. Cell. Proteomics. 1, 816-827. 

Nechushtai, R., Muster, P., Binder, A., Liveanu, V. and Nelson, N. 1983. Photosystem I reaction center from the thermophilic cyanobacterium Mastigocladus laminosus. Proc. Acad. Sci. U.S.A., 80. 1179-1183. 

Figure 19 (a) Crystal structure of the c)ftochrome b f complex from Mastigocladus laminosus at 3.0 A resolution. The coordinates were obtained from the Protein Data Bank and visualized using accefrys DSViewer Pro. (b) The electron and proton transfer chain of c)dochrome i>6 / with the protein stripped away... 

Fig, 13. Three-dimensional structure of C-phycocyanin (C-PC) o-subunit and j8-subunit (A and B) and o/3-trimer (C) derived from X-ray diffraction analysis of crystals of C-PC isolated from the cyanobacterium Mastigocladus laminosus (Fischerella PCC 7603) (101,145]. The possible positions of the additional PEB chromophores in C-PE from Fremyella diplosiphon (Calothrix UTEX 481) are adapted to the models of C-PC, using data from the amino acid sequence of C-PE [115]. Positions of the PEB chromophores at cysteine 50/61 X-X and 143a X. The beginning of the insertion 141a-o in J-C-PE is indicated by an arrow (— ). 

The subject of energy transfer in phycobilisomes and their sub-structures already has a large literature (see Ref. 65 for a review), mostly beyond the scope of this chapter. However, two of these sub-structures - trimeric C-phycocyanin from the thermophilic cyanobacterium Mastigocladus laminosus and hexameric C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum-have very recently become respectively the third and fourth photosynthetic pigment-protein complexes for which structural models based on single-crystal X-ray diffraction near atomic resolution are now available (Refs. 66,67 and Chapter 11). Since these are presently the only such complexes, in addition to the two already discussed (Sections 5 and 6), it seems appropriate to conclude this review of exciton effects with some brief remarks on these C-phycocyanin structures. 

Figure 2.12. Overall structure of the dimer cytochrome h/, as measured by X-ray scattering for the thermophilic cyanobacteriiun Mastigocladus laminosus. Its position relative to the thylakoid membrane is indicated in Fig. 2.14. Resolution 0.3 nm. Based on Protein Data Bank ID 1UM3 (Kurisu et al, 2003).

Once the reaches cytochrome b f and gets close to a protoporph rm heme molecule, the two protons are released and plastoquinone is recycled to the photosystem II. Figure 2.22 shows the overall structure of the cyanobacterium Mastigocladus laminosus cytochrome b f (Kurisu et ah, 2003), which together with the structure derived from the alga Clamydomonas reinhardtii (Stroebel et ah, 2003) is the most recent element in completion of the photo-... 

X-ray crystallographic analysis of C-phycocyanin from Mastigocladus laminosus (a thermophilic cyanobacterium) shows the phycobiliprotein to be a doughnut-shaped trimer [see Fig. 7 below]. The a-and (3-isubunits have tertiary structures that are similar to one another, consistent with their sequence... 

Fig. 6. Top Schematic representation ofthe assembly of phycobiliprotein trimers and hexamers from the a- and p-subunits (same as Fig. 2). (A) Stereogram ofthe C-PC p-subunit (B) stereogram of the C-PC(ap)-monomer. Helices are represented by cylinders those ofthe p-subunit are labeled with uppercase letters and those ofthe a-subunit with lowercase letters. Chromophores in (A) and (B) are represented by wire models. Figure source (A) and (B) Schirmer, Bode, Huber, Sidler and Zuber (1985) X-ray crystallographic structure of the light-harvesting biliprotein C-phycocyanin from the thermophilic cyanobacterium Mastigocladus laminosus and its resemblance to globin structures. J Mol Biol 184 268,272.

M Mimuro, P Fglistaller, R Rmbeli and H Zuber (1986) Eunctional assignment of chromophores and energy transfer in C phycocyanin isolated from the thermophilic cyanobacterium Mastigocladus laminosus. Biochim Biophys Acta 848 155-166... 

STUDIES ON THE ROD-SUBSTRUCTURE OF THE PHICOBILISOME FROM THE CIANOBACTERIUM MASTIGOCLADUS LAMINOSUS>... 

Fig. 4. Previous (A) and updated (B) model of the phycobilisome of Mastigocladus laminosus showing the location and polypeptide composition (phycobiliproteins, linker polypeptides) of the complexes making up the r s and the three-cylinder core. (1) Lr -, ...

ISOLATION AND CHARACTERIZATION OF THE ALLOPHICOCTANIN COMPLEXES OF THE CIANOBACTERIDM MASTIGOCLADUS LAMINOSUS... 

Allophycocyanin from Mastigocladus laminosus is a blue water-soluble pigment protein-complex and a component of the phycobilisome core. The aggregates of core phycobiliproteins are trimeric complexes as shown below ... 

PHOTOSYSTEM I REACTION CENTER OF MASTIGOCLADUS LAMINOSUS STRUCTURAL AND FUNCTIONAL ASPECTS... 

Growing the plants and the cyanobacteria Spinach was grown hydroponically at 25 C with 16 hour light and 8 hour dark cycles. Mastigocladus laminosus was grown at 55X, under continuous illumination (30 Ei/ cm lsec ) as described before (18). 

In the present work we characterized several forms of Mastigocladus laminosus PS-I-RC crystals. 

Table 2 Comparison of photochemistry of PEC between Mastigocladus laminosus and Chroococcidiopsis spec.

Studies on the Rod-Substructure of the Phycobilisome from the Cyanobacterium Mastigocladus laminosus 89... 

Isolation and Characterization of the Allophycocyanin Complexes of the Cyanobacterium Mastigocladus laminosus 93... 

Photosystem I Reaction Center of Mastigocladus Laminosus Structural and Functional... 

Photosystem I reaction centers from spinach, Swiss chard Chlamydomonas reinhardii, and Mastigocladus laminosus were purified as described in (Nechushtai et al. 1981 Nechushtai, Nelson 1981) and (Nechushtai et al. 1983) respectively. Greening experiments in dark grown spinach oat and bean plants were performed as previously described (Nechushtai, Nelson 1983). 

The isolation and characterisation of subunit 1 as a fully active photosystem 1 reaction center by its own is described by Binder et al. (this symposium). Analogous to the study on the binding site of the nonheme iron in Rho do spirillum rubrum we tried to localize the iron binding site of photosystem 1 reaction center of Mastigocladus laminosus. 

We have isolated reaction center 1 of Mastigocladus laminosus cells labeled with the isotope 39-Fe. The exact subunit composition of this reaction center is still a matter of discussion (see Binder et al., this symposium). At room temperature (25 C) the reaction center 1 does not dissociate into the subunits with apparent molecular weight of 70 kDal and 30 kDal, respectively (Figure 2). 

Figure 2 LDS-poIyacrylamide gel electrophoresis of Mastigocladus laminosus reaction center 1 Varying temperature and incubation time during sample preparation. Explanations see text.

In an earlier communication (Nechushtai et al. 1983) we reported on the purification of the photosystem I reaction center from the thermophilic cyanobacterium Mastigocladus laminosus. The subunit composition and the photochemical properties of this reaction center were compared with those of photosystem I reaction centers from green algae and higher plants. Immunological crossreactivity between subunits 1 as well as between subunits II from these different sources was indicated and its evolutional significance was discussed. 

We describe here the isolation and characterization of subunit I of Mastigocladus laminosus as a fully active photosystem I reaction center by its own. 

Fuglistaller P, Widmer H, Sidler W, Frank G and Zuber H (1981) Isolation and characterization of phycoerythrocyanin and chromatic adaptation of the thermophilic Cyanobacterium Mastigocladus laminosus. Arch. Microbiol. 129, 268-274. 

Nies M and Wehrmeyer W (1980) Isolation and biliprotein characterization of phycobilisomes from the thermophilic Cyanobacterium Mastigocladus laminosus Cohn. Planta 150, 330-337. 

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