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Biliproteins of Cyanobacteria and Rhodophyta

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Biliproteins of Cyanobacteria and Rhodophyta Proc. Nat. Acad. Sci. USA Vol. 78, No. 2, pp. 428-431, February 1976 Biochemistry Biliproteins of cyanobacteria and Rhodophyta: Homologous family of photosynthetic accessory pigments (phycobiliproteins/amino-terminal sequences/evolution/structure-function relationships) ALEXANDER N. GLAZER, GERALD S. APELL, CRAIG S. HIXSON, DONALD A. BRYANT, SARA RIMON*, AND DOUGLAS M. BROWN Department of Biological Chemistry, UCLA School of Medicine, and the Molecular Biology Institute, University of California, Los Angeles, Calif. 90024 Communicated by Emil L. Smith, December 1, 1975 ABSTRACT Amino-terminal sequence determinations carrying chromophore(s) (see Table 1). The molecular are re orted of the subunits of biliproteins of prokaryotic weights of the a and f3 subunits differ among the bilipro- unicel ular and filamentous cyanobacteria and of eukaryotic teins, and depend on the source organism, but, strikingly, all unicellular red algae. The biliproteins examined, allophyco- cyanin, -phycocyanin, R-phycocyanin, b-phycoerythrin, and fall in the approximate range of 14,000-20,000 (2). The phycoerythrocyanin, vary with respect to the chemical na- prosthetic groups are invariably open chain tetrapyrroles (2). ture and the number and distribution of the bilin chromo- These observations lead to the postulation of a common phores between the two dissimilar subunits. The amino-ter- ancestral gene for this group of proteins (10). This hypothe- minal sequences fall into two classes, "a-type" and ",-type", sis is supported by the sequence data presented here. with a high degree of homology within each class. In those biliproteins where the number of bilin chromo- phores on the two subunits is unequal, the subunit with the MATERIALS AND METHODS greater number of chromophores has the j#-type amino-acid The unicellular blue-green alga Microcystis aeruginosa sequence. ATCC 22663 was obtained from the American Type Cul- Extensive homology also exists between a- and #-type se- quences, strongly supporting the view that these arose by ture Collection, Rockville, Md., and maintained in medium gene duplication to give rise to the ancestral a- and a-type BG 11, as described by Stanier et al. (11). The cells were genes early in the evolution of the biliproteins. The subse- grown to a density of approximately 1.5 g/liter and harvest- quent generation of the various classes of biliproteins ap- ed by centrifugation, and the pellets were stored at -20°. pears to be the result of further gene duplication of the a- The source of the organisms and the preparation of the and a-type genes, ultimately to give rise to families of poly- biliprotein fractions from Anabaena variabilis and Porphy- peptide chains of similar sequence, but varying in the num- cruentum B been 3). Al- ber of chromophore attachment sites and the structure of the ridium has described previously (1, chromophores. lophycocyanins and C-phycocyanins were purified by the general procedures described previously (4, 9). R-Phyco- The phycobiliproteins are the major light-harvesting pig- cyanin was purified by the procedure of Glazer and Hixson ments of photosystem II of cyanobacteria and Rhodophyta. (1). The details of the purification of phycoerythrocyanin (3) Three major classes of biliproteins have been recognized for and b-phycoerythrin (12) will be described elsewhere. a number of years: the allophycocyanins (Xmax 650 nm), and The subunits of C-phycocyanin, R-phycocyanin, and phy- C-phycocyanins (Xmax about 620 nm), both of which carry coerythrocyanin were separated by the method of Glazer covalently bound phycocyanobilin (PCB) prosthetic groups, and Fang (3), by stepwise elution from Bio-Rex 70 at pH 3.0 and phycoerythrins (Xmax about 565 nm) with covalently at- with solutions of increasing urea concentration. Allophyco- tached phycoerythrobilin (PEB) groups. R-Phycocyanins, cyanin subunits were separated by chromatography on found in certain red algae, carry both PCB and PEB DEAE-Sephadex A-50 at pH 8.0 in 8 M urea, by the proce- moieties. The nomenclature and properties of biliproteins dure of Gysi and Zuber (13), but with stepwise rather than have been reviewed recently (1, 2). gradient elution. The fl subunit was eluted with 8 M urea- There are two other types of cyanobacterial biliproteins: allophycocyanin B (Xmax about 670 nm) (3), and phycoer- ythrocyanin (Xmax 568 nm) (ref. 3, and unpublished observa- Table 1. Type and number of bilin chromophores on the tions). subunits of various biliproteins Within a given class of biliproteins, e.g., C-phycocyanins, there is a remarkable conservation of physical and immuno- ai-type logical properties (2, 4-6), primary structure (7), and chro- Protein subunit (3-type subunit Ref. mophore content (8). Indeed, hybrid proteins have been suc- cessfully reconstituted from the subunits of C-phycocyanins Allophycocyanin 1 PCB 1 PCB 8 derived from unrelated organisms (9). C-Phycocyanin 1 PCB 2 PCB 8 The various classes of biliproteins also exhibit several com- R-Phycocyanin 1 PCB 1 PCB and 1 1 PEB mon characteristics. The monomer species is in each in- Phycoerythrocyanin PXB* 2 PCB * stance made up of two dissimilar subunits, a and (,B each b-Phycoerythrin 2 PEB 3-4 PEB t Abbreviations: PCB, phycocyanobilin; PEB, phycoerythrobilin; * PXB is a phycoerythrobilin-type chromophore (Xmax 330 and 590 PXB, a phycoerythrobilin-type chromophore of undetermined nm, in 8 M urea at pH 3.0) of as yet undetermined structure (D. A. structure. Bryant, F. E. Eiserling, and A. N. Glazer, unpublished observa- * Present address: Biochemistry Department, Tel-Aviv University, tions). Israel. t A. N. Glazer and C. S. Hixson, unpublished observations. 428 Downloaded by guest on September 28, 2021 Biochemistry: Glazer et al. Proc. Nat. Acad. Sci. USA 73 (1976) 429 Table 2. Percentage yields of certain phenylthiohydantoin derivatives obtained on sequential Edman degradation of biliprotein subunits Residue number - mol Source Protein 1 2 3 4 5 6 7 8 9 10 11 12 14 15 16 17 18 19 used Synechococcus 45 23 21 56 22 17 24 21 0.27 sp. 6301 Allophycocyanin (3 M. aeruginosa Allophycocyanin a 20 14 19 12 9 9 13 12 5 0.43 M. aeruginosa Allophycocyanin , 35 10 20 15 12 10 0.10 A. variabilis Allophycocyanin a 33 44 19 15 26 22 13 7 13 0.73 A. variabilis Allophycocyanin 3 52 52 26 16 35 26 52 26 31 4 8 0.62 P. cruentum Allophycocyanin a 19 6 6 12 6 3 8 5 0.31 P. cruentum Allophycocyanin 41 47 41 47 23 23 17 17 0.35 P. cruentum R-Phycocyanin a 67 34 67 34 34 55 0.24 P. cruentum R-Phycocyanin 3 63 51 32 51 29 32 32 17 8 0.24 P. cruentum b-Phycoerythrin a 38 76 29 38 19 10 19 19 0.21 P. cruentum b-Phycoerythrinj3 51 51 32 32 32 10 11 11 22 13 0.31 A. variabilis Phycoerythrocyanin ct 6 6 8 10 8 8 8 0.48 A. variabilis Phycoerythrocyanin 3 41 17 17 22 17 11 0.36 0.01 M K-phosphate-0.01 M 2-mercaptoethanol-0.05 M acid, or heptafluorobutyric acid). An aliquot was withdrawn NaCI at pH 8.0, and the a with the same buffer containing for quantitative amino-acid analysis and the remainder was 0.18 M NaCl. The subunits of b-phycoerythrin were sepa- added to the spinning cup at high speed (1600 rpm at 55°). rated by chromatography on CM-cellulose at pH 5.0 in 8 M The sample container was washed with 0.1 ml of solvent and urea with a NaCl gradient (Glazer and Hixson, manuscript the washings were added to the cup. The modifications to in preparation). Beckman Program 122974 were as follows: double coupling The sequential Edman degradation was performed in a on the first cycle, and increase in the restricted vacuum dry- Beckman sequencer model 890-C using the Beckman Pro- down times at program steps 19, 25, 31, 41, and 48-400, 200, tein Quadrol Program 122974 ("In Sequence", Issue No. 8, 260, 300, and 260 sec, respectively. Nitrogen dry-down at Oct. 1975, Beckman Instruments, Inc.), and 0.2 M quadrol program step 30 was increased from 30 to 230 sec. (single cleavage). Lyophilized polypeptide (0.1-0.75 ,mol) The butyl chloride extracts containing the anilinothiazoli- was dissolved in about 0.3 ml of an appropriate solvent (30% nones were dried under nitrogen at 50°, and conversion to vol/vol acetic acid, 70% vol/vol formic acid, trifluoroacetic the phenylthiohydantoin derivatives was accomplished with Table 3. Amino-terminal sequences of biliprotein subunits* a-type subunits 1 5 10 15 Synechococcus sp. 6301 C-Phycocyanin a Subunitt Ser-Lys-Thr-Pro-Leu-( )-Glu-Ala-Val-Ala-Ala-Ala-Asx-( )-( )-Gly Anabaena variabilis C-Phycocyanin a Subunit Val-Lys-Thr-Pro-fle-Thr-Glu-Ala-Be-Ala-( )-Ala-( )-Asp-Gln-Gly-Arg-Phe-Leu-Gly-Asn Mastigocladus laminosus C-Phycocyanin a Subunit § Val-Lys-Thr-Pro-Ile-Thr-Asp-Ala-le-Ala-Ala-Ala-Asp-Thr-Gln-Gly-Arg-Phe-Leu-Ser-Asn-Thr-Glu Cyanidium caldarium C-Phycocyanin a Subunit¶ Met-Lys-Thr-Pro-lle-Thr-Glu-Ala-lle-Ala-Ala-Ala-Asx(Ala)Arg-Gly Porphyridium cruentum R-Phycocyanin a Subunit Met-Lys-Thr-Pro-Ile-Thr-Glu-Ala-Ile-Ala-Thr-Ala-Asp-Asn-Gln-Gly-Arg-Phe-Leu-( )Asn Anabaena variabilis Phycoerythrocyanin a Subunit Met-Lys-Thr-Pro-Leu-Thr-Glu-Ala-Ile-Gly-Ala-Ala-Asp-Val-Arg-Gly-( )-Tyr-Leu-( )-Asn Porphyridium cruentum b-Phycoerythrin a Subunit Met-Lys-Ser-Val-Ile-( }Thr-Val-Val-( -Ala-Ala-Asp-Ala-Ala-Gly(Arg)Phe-Pro 1 5 10 15 (Ble/I 20 Microcystis aeruginosa Allophycocyanin a Subunit Ser-Ile-Val-Thr-Lys-( )fle-Val-Asn-Ala-Asp-Ala-Glu-Ala-Arg-Tyr-Leu\Leu/Pro-Gly-Glu Anabaena variabilis Allophycocyanin a Subunit ( )-lle-Val-( )-Lys-( )-lle-Val-Asn-Ala-Asp-Ala-Glu-Ala-( )-Tyr-Leu-Leu Porphyridium cruentum Allophycocyanin ca Subunit Ser-lle-Val-Thr-Lys-( )-fIle-Val-Asn-Ala-Asp-Ala-Glu-Ala-Arg-Tyr-Leu ,-type subunits Synechococcus sp.
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