Genes for phycocyanin subunits in Synechocystis sp. strain PCC 6701 and assembly mutant UV16.
نویسندگان
چکیده
The cyanobacterial phycobilisome is a large protein complex located on the photosynthetic membrane. It harvests light energy and transfers it to chlorophyll for use in photosynthesis. Phycobilisome assembly mutants in the unicellular cyanobacterium Synechocystis sp. strain 6701 have been characterized. One such mutant, UV16, contains a defect in the assembly of the biliprotein phycocyanin. We report the cloning and sequencing of the phycocyanin genes from wild-type Synechocystis strain 6701 and demonstrate an alteration in the gene for the phycocyanin alpha subunit in UV16. Possible consequences of the lesion on phycobilisome assembly were assessed from its position in the phycocyanin tertiary and quaternary structures. The UV16 phenotype is complex and includes a reduced level of phycocyanin relative to that in the wild type. To determine whether the lower phycocyanin content results from lower transcript levels, a fragment of cpcBA was used as a probe for quantitating phycocyanin mRNA. Both the wild type and UV16 contained two phycocyanin transcripts of approximately 1.4 and 1.5 kilobases that were equal in abundance and that did not vary with light quality during cell growth. Equal levels of these transcripts in the wild type and UV16 suggest that the lower phycocyanin content in the mutant may be due to posttranscriptional events. The 5' ends of the two phycocyanin mRNAs were mapped at 100 and 223 base pairs upstream of the cpcB initiation codon. Homologous regions upstream of the putative transcription initiation sites may be important for maintaining high levels of transcription from the Synechocystis strain 6701 phycocyanin gene set.
منابع مشابه
CpcM posttranslationally methylates asparagine-71/72 of phycobiliprotein beta subunits in Synechococcus sp. strain PCC 7002 and Synechocystis sp. strain PCC 6803.
Cyanobacteria produce phycobilisomes, which are macromolecular light-harvesting complexes mostly assembled from phycobiliproteins. Phycobiliprotein beta subunits contain a highly conserved gamma-N-methylasparagine residue, which results from the posttranslational modification of Asn71/72. Through comparative genomic analyses, we identified a gene, denoted cpcM, that (i) encodes a protein with s...
متن کاملCyanobacterial 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, 30.5, and 27 x 10(3) Daltons, as well as a trace of a approximately 9 x 10(3)-dalton component. Two nitrosoguanidine-induced mutants of this organi...
متن کاملRod substructure in cyanobacterial phycobilisomes: phycoerythrin assembly in synechocystis 6701 phycobilisomes
Synechocystis 6701 phycobilisomes consist of a core of three cylindrical elements in an equilateral array from which extend in a fanlike manner six rods, each made up of three to four stacked disks. Previous studies (see Gingrich, J. C., L. K. Blaha, and A. N. Glazer, 1982. J. Cell Biol. 92:261-268) have shown that the rods consist of four disk-shaped complexes of biliproteins with "linker" pol...
متن کاملRod 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-, 30.5-, and 27-kdaltons. Wild-type phycobilisomes consist of a core of three cylindrical elements in an equilateral array surrounded by a fanlike array of six rods each made up of 3-4 stacked disks. Twelve nitrosoguan...
متن کاملAllophycocyanin and phycocyanin crystal structures reveal facets of phycobilisome assembly.
X-ray crystal structures of the isolated phycobiliprotein components of the phycobilisome have provided high resolution details to the description of this light harvesting complex at different levels of complexity and detail. The linker-independent assembly of trimers into hexamers in crystal lattices of previously determined structures has been observed in almost all of the phycocyanin (PC) an...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of bacteriology
دوره 172 3 شماره
صفحات -
تاریخ انتشار 1990