N-Terminus Conservation in the Terminal Pigment of Phycobilisomes from a Prokaryotic and Eukaryotic Alga 1
AUTOR(ES)
Gantt, Elisabeth
RESUMO
High molecular weight polypeptides from phycobilisomes, believed to be involved in facilitating the energy flow from phycobilisomes to thylakoids, are conserved in the prokaryote Nostoc sp. and the eukaryote Porphyridium cruentum. Partial N-terminal sequence analysis of the phycobilisome-polypeptides of Nostoc (94 kilodalton) and Porphyridium (92 kilodalton) revealed 55% identity in the first 20 residues, but no significant homology with sequences of other phycobiliproteins or phycobilisome-linkers. Polypeptides (94 and 92 kilodalton) from Nostoc thylakoids free of phycobilisomes, previously presumed to be involved in the phycobilisome-thylakoid linkage (M Mimuro, CA Lipschultz, E Gantt 1986 Biochim Biophys Acta 852: 126) exhibit the same immunocrossreactivity but are different from the 94 kilodalton-phycobilisome polypeptide by having blocked N-termini and a different amino acid composition.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1054615Documentos Relacionados
- Key role of the N-terminus of chicken annexin A5 in vesicle aggregation
- Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3
- Interaction between the N-terminus of human topoisomerase I and SV40 large T antigen.
- The major form of MeCP2 has a novel N-terminus generated by alternative splicing
- Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo