presence of multidomain linkers determines the bundle-shape structure of the phycobilisome of the cyanobacterium Gloeobacter violaceus PCC 7421

The complete genome sequence of Gloeobacter violaceus [Nakamura et al. (2003a, b) DNA Res 10:37-45, 181-201] allows us to understand better the structure of the phycobilisomes (PBS) of this cyanobacterium. Genomic analysis revealed peculiarities in these PBS: the presence of genes for two multidomai...

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Bibliographic Details
Published in:Photosynthesis research 2007-07, Vol.93 (1-3), p.27-43
Main Authors: Krogmann, David W, Pérez-Gómez, Bertha, Gutiérrez-Cirlos, Emma Berta, Chagolla-López, Alicia, González de la Vara, Luis, Gómez-Lojero, Carlos
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Bacteria
Bacterial Proteins - chemistry
Centrifugation, Density Gradient
Cyanobacteria
Cyanobacteria - chemistry
Cyanobacteria - genetics
Cyanobacterium
Cyanophyta
Ferredoxin
Gel electrophoresis
Genes, Bacterial
Genomic analysis
Genomics
Gloeobacter violaceus
Hexamers
Membrane proteins
Models, Biological
Molecular Sequence Data
Multidomain linkers
NADP
Nucleotide sequence
Oxidoreductase
Peptide mapping
phycobilisome
Phycobilisomes
Phycobilisomes - chemistry
Porins - chemistry
Protein Structure, Tertiary
Protein Subunits - chemistry
Protein Subunits - isolation & purification
Protein Transport
Rods
Sequence Alignment
Trimers
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Summary:The complete genome sequence of Gloeobacter violaceus [Nakamura et al. (2003a, b) DNA Res 10:37-45, 181-201] allows us to understand better the structure of the phycobilisomes (PBS) of this cyanobacterium. Genomic analysis revealed peculiarities in these PBS: the presence of genes for two multidomain linker proteins, a core membrane linker with four repetitive sequences (REP domains), the absence of rod core linkers, two sets of phycocyanin (PC) α and β subunits, two copies of a rod PC associated linker (CpcC), and two rod cap associated linkers (CpcD). Also, there is one ferredoxin-NADP⁺ oxidoreductase with only two domains. The PBS proteins were investigated by gel electrophoresis, amino acid sequencing and peptide mass fingerprinting (PMF). The two unique multidomain linkers contain three REP domains with high similarity and these were found to be in tandem and were separated by dissimilar Arms. One of these, with a mass of 81 kDa, is found in heavy PBS fragments rich in PC. We propose that it links six PC hexamers in two parallel rows in the rods. The other unique linker has a mass of 91 kDa and is easily released from the heavy fragments of PBS. We propose that this links the rods to the core. The presence of these multidomain linkers could explain the bundle shaped rods of the PBS. The presence of 4 REP domains in the core membrane linker protein (129 kDa) was established by PMF. This core linker may hold together 16 AP trimers of the pentacylindrical core, or alternatively, a tetracylindrical core of the PBS of G. violaceus.
ISSN:0166-8595
1573-5079
DOI:10.1007/s11120-007-9133-9