Cyanobacterial phycobilisomes. Role of the linker polypeptides in the assembly of phycocyanin.

The phycocyanin-containing segments of the rod substructures of Anabaena variabilis phycobilisomes consist of complexes of phycocyanin with "linker" polypeptides of 27,000 and 32,500 daltons (Yu, M.-H., Glazer, A.

Rod substructure in cyanobacterial phycobilisomes: analysis of Synechocystis 6701 mutants low in phycoerythrin.

Synechocystis 6701 phycobilisomes contain phycoerythrin, phycocyanin, and allophycocyanin in a molar ratio of approximately 2:2:1, and other polypeptides of 99-, 46-, 33.5-, 31.5-, 30.

Cyanobacterial phycobilisomes. Phycocyanin assembly in the rod substructures of anabaena variabilis phycobilisomes.

Phycocyanin complexes with "linker" polypeptides (Lundell, D. J., Williams, R.

Allophycocyanin B. A common beta subunit in Synechococcus allophycocyanin B (lambda max 670 nm) and allophycocyanin (lambda max 650 nM).

In cyanobacterial phycobilisomes, light energy absorbed by phycocyanin (lambda max 620 nm) is transferred to allophycocyanin (AP; lambda max 650 nm) and allophycocyanin B (AP-B; lambda max 670 nm) and emitted primarily at 680 nm. This emission maximum coincides with that of pure AP-B. Previous studies have shown that Synechococcus 6301 AP and AP-B are both (alpha beta)3 trimers with a number of similar properties.

A terminal energy acceptor of the phycobilisome: the 75,000-dalton polypeptide of Synechococcus 6301 phycobilisomes--a new biliprotein.

A rapid procedure is described for the isolation of "linker" polypeptides (Lundell, D. J., R.

The amino acid sequence of the beta subunit of allophycocyanin.

The complete amino acid sequence of the beta subunit of Anabaena variabilis allophycocyanin is: H2N-Ala-Gln-Asp-Ala-Ile-Thr-Ala-Val-Ile-Asn-Ser-Ala-Asp-Val-Gln-Gly-Lys-Tyr-Leu-Asp-Thr-Ala-Ala-Leu-Glu-Lys-Leu-Lys-Ala-Tyr-Phe-Ser-Thr-Gly-Glu-Leu-Arg-Val-Arg-Ala-Ala-Thr-Thr-Ile-Ser-Ala-Asn-Ala-Ala-Ala-Ile-Val-Lys-Glu-Ala-Val-Ala-Lys-Ser-Leu-Leu-Tyr-Ser-Asp-Ile-Thr-Arg-Pro-Gly-Gly-Asn-Met-Tyr-Thr-Thr-Arg-Arg-Tyr-Ala-Ala-Cys-Ile-Arg-Asp-Leu-Asp-Tyr-Tyr-Leu-Arg-Tyr-Ala-Thr-Tyr-Ala-Met-Leu-Ala-Gly-Asp-Pro-Ser-Ile-Leu-Asp-Glu-Arg-Val-Leu-Asn-Gly-Leu-Lys-Glu-Thr-Tyr-Asn-Ser-Leu-Gly-Val-Pro-Val-Gly-Ala-Thr-Val-Gln-Ala-Ile-Gln-Ala-Ile-Lys-Glu-Val-Thr-Ala-Ser-Leu-Val-Gly-Ala-Asp-Ala-Gly-Lys-Glu-Met-Gly-Ile-Tyr-Leu-Asp-Tyr-Ile-Ser-Ser-Gly-Leu-Ser-COOH Phycocyanobilin is attached though a thioether linkage to cysteinyl residue 81, indicated by an asterisk. Comparison of this sequence with those of C-phycocyanins shows that there are 60 identities between corresponding subunits of these two biliproteins. Of the region between residues 79 and 120, 29 residues are identical in the beta subunits of allophycocyanin and phycocyanin.

Phycoerythrins of the Red Alga Callithamnion: VARIATION IN PHYCOERYTHROBILIN AND PHYCOUROBILIN CONTENT.

Phycoerythrins of several species of the higher red alga Callithamnion show virtually identical spectra, typical of R-phycoerythrins, with absorption maxima at 565, 539, and 497 nanometers. One species, Callithamnion roseum, produces a phycoerythrin lacking the peak at 539 nanometers. Comparison of a "typical" R-phycoerythrin from Callithamnion byssoides with the "atypical" phycoerythrin of C.

Molecular architecture of a light-harvesting antenna. In vitro assembly of the rod substructures of Synechococcus 6301 phycobilisomes.

The 75-, 33-, 30-, and 27-kilodalton polypeptide components ("linker polypeptides") of the phycobilisome of the unicellular cyanobacterium Synechococcus 6301 have been purified and characterized. In 0.6 M NaK phosphate buffer at pH 8, the 33-, 30-, and 27-kilodalton polypeptides assemble phycocyanin into ordered aggregates, whereas the 75-kilodalton polypeptide does not interact with phycocyanin.

Molecular architecture of a light-harvesting antenna. Comparison of wild type and mutant Synechococcus 6301 phycobilisomes.

Phycobilisomes of the cyanobacterium Synechococcus 6301 contain C-phycocyanin and allophycocyanin in a molar ratio of approximately 3.8:1, a minor biliprotein, allophycocyanin B, and nonpigmented polypeptides of 75, 33, 30, and 27 kilodaltons. A nitrosoguanidine-induced mutant AN112 produces altered phycobilisomes with the molar ratio of C-phycocyanin to allophycocyanin reduced to approximately 1.

Cyanobacterial phycobilisomes. Particles from Synechocystis 6701 and two pigment mutants.

The phycobilisomes of the unicellular cyanobacterium Synechocystis 6701, grown in white light, contain C-phycoerythrin, C-phycocyanin, and allophycocyanin in a molar ration of approximately 2:2:1, and in addition, polypeptides of 99, 46, 33.5, 31.5, 30.

Characterization of cyanobacterial phycobilisomes in zwitterionic detergents.

Properties of cyanobacterial phycobilisomes (from Synechococcus spp. 6301 and 6312 and Synechocystis sp. 6701) prepared in the presence of two different zwitterionic detergents were compared to those of phycobilisomes detached from membranes with the nonionic detergent Triton X-100 and then freed from Triton by sedimentation through high-salt sucrose density gradients.

Cyanobacterial phycobilisomes. Characterization of the phycobilisomes of Synechococcus sp. 6301.

A procedure is described for the preparation of stable phycobilisomes from the unicellular cyanobacterium Synechococcus sp. 6301 (also known as Anacystis nidulans). Excitation of the phycocyanin in these particles at 580 nm leads to maximum fluorescence emission, from allophycocyanin and allophycocyanin B, at 673 nm.

Preliminary crystallographic investigations of two phycobiliproteins.

Single crystal x-ray diffraction investigations are in progress on two phycobiliproteins. C-phycocyanin from Anabaena variabilis crystallizes in space group P63 with a = b = 154 A and c = 40 A. The crystallographic asymmetric unit is (alphabeta)2 with a total molecular mass of 7.

Classification of Bacillus subtilis flagellins.

Purified flagellins derived from 16 strains of Bacillus subtilis were classified into at least five distinct groups on the basis of their reaction with antiflagellar filament antibody and antiflagellin antibody. This classification was in good accord with that derived independently on the basis of amino acid analyses of the flagellins. Flagellar antigenicity appears to provide a useful typological character in classifying B.

Physico-chemical and immunological properties of allophycocyanins.

Allophycocyanins were purified from diverse cyanobacteria and one rhodophytan alga (Cyanidium caldarium). The native proteins are trimeric molecules with the structure (alpha beta)3. Representative native allophycocyanins and their alpha and beta subunits were characterized with respect to molecular weight, amino acid composition, isoelectric point, absorption and fluorescence spectra and immunological properties.

Subunit structure and chromophore composition of rhodophytan phycoerythrins. Porphyridium cruentum B-phycoerythrin and b-phycoerythrin.

A comparative study is presented of the two phycoerythrins of the unicellular red alga Porphyridium cruentum. Native B-phycoerythrin has a molecular weight of 236,000 +/- 18,000 in 0.05 M potassium phosphate at pH 7.

Characterization and structural properties of the major biliproteins of Anabaena sp.

Studies are presented of the biliproteins of Anabaena sp. This filamentous cyanobacterium contains three major biliproteins. Whereas two of these, C-phycocyanin and allophycocyanin, are common to all cyanobacteria, the third, phycoerythrocyanin (gammamax approximately 568 nm) has hitherto not been described and its distribution among cyanobacteria appears to be limited.