Borrowed proteins in bacterial bioluminescence. Export

@article{citeulike:5041242, abstract = {A library of Photobacterium phosphoreum DNA was screened in lambda 2001 for the lumazine protein gene, using two degenerate 17-mer oligonucleotide probes that were deduced from a partial protein primary sequence. The lumazine protein gene was localized to a 3.4-kilobase BamHI/EcoRI fragment in one clone. The fragment contained an open reading frame, encoding a 189-residue protein, that had a predicted amino acid sequence that concurred with the partial sequence determined for lumazine protein. Considerable sequence similarity was detected between lumazine protein, the yellow fluorescence protein from Vibrio fischeri, and the alpha subunit of riboflavin synthetase (EC 2.5.1.9). A highly conserved sequence in lumazine protein corresponds to the proposed lumazine binding sites in the alpha subunit of riboflavin synthetase. Several secondary structure programs predict the conformation of this site in lumazine protein to be a beta-sheet. A minimal model with three interactions between the ligand and this beta-sheet structure is proposed, which is consistent with the results of NMR and ligand binding studies.}, author = {O'Kane, D. J. and Woodward, B. and Lee, J. and Prasher, D. C.}, citeulike-article-id = {5041242}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/1996310}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=1996310}, issn = {0027-8424}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {bacteria, bioluminescence, fluorescence, lumazine, proteins, riboflavin, yfp}, month = {February}, number = {4}, pages = {1100--1104}, posted-at = {2009-07-02 12:19:56}, priority = {2}, title = {Borrowed proteins in bacterial bioluminescence.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/1996310}, volume = {88}, year = {1991} }

TY - JOUR ID - citeulike:5041242 L3 - citeulike-article-id:5041242 N2 - A library of Photobacterium phosphoreum DNA was screened in lambda 2001 for the lumazine protein gene, using two degenerate 17-mer oligonucleotide probes that were deduced from a partial protein primary sequence. The lumazine protein gene was localized to a 3.4-kilobase BamHI/EcoRI fragment in one clone. The fragment contained an open reading frame, encoding a 189-residue protein, that had a predicted amino acid sequence that concurred with the partial sequence determined for lumazine protein. Considerable sequence similarity was detected between lumazine protein, the yellow fluorescence protein from Vibrio fischeri, and the alpha subunit of riboflavin synthetase (EC 2.5.1.9). A highly conserved sequence in lumazine protein corresponds to the proposed lumazine binding sites in the alpha subunit of riboflavin synthetase. Several secondary structure programs predict the conformation of this site in lumazine protein to be a beta-sheet. A minimal model with three interactions between the ligand and this beta-sheet structure is proposed, which is consistent with the results of NMR and ligand binding studies. IS - 4 JF - Proceedings of the National Academy of Sciences of the United States of America SN - 0027-8424 EP - 1104 TI - Borrowed proteins in bacterial bioluminescence. VL - 88 SP - 1100 KW - bacteria KW - bioluminescence KW - fluorescence KW - lumazine KW - proteins KW - riboflavin KW - yfp AU - O'Kane, DJ AU - Woodward, B AU - Lee, J AU - Prasher, DC PY - 1991/02/15/ UR - http://view.ncbi.nlm.nih.gov/pubmed/1996310 ER -