Adaptive evolution of multicolored fluorescent proteins in reef-building corals

被引:83
作者
Field, SF
Bulina, MY
Kelmanson, IV
Bielawski, JP
Matz, MV
机构
[1] Univ Florida, Whitney Lab Marine Biosci, St Augustine, FL 32080 USA
[2] Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow, Russia
[3] Dalhousie Univ, Dept Biol, Halifax, NS, Canada
[4] Univ Florida, Dept Mol Genet & Microbiol, Gainesville, FL 32610 USA
关键词
green fluorescent protein; fluorescence; color evolution; positive selection; symbiosis;
D O I
10.1007/s00239-005-0129-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Here we investigate the evolutionary scenarios that led to the appearance of fluorescent color diversity in reef-building corals. We show that the mutations that have been responsible for the generation of new cyan and red phenotypes from the ancestral green were fixed with the help of positive natural selection. This fact strongly suggests that the color diversity is a product of adaptive evolution. An unexpected finding was a set of residues arranged as an intermolecular binding interface, which was also identified as a target of positive selection but is nevertheless not related to color diversification. We hypothesize that multicolored fluorescent proteins evolved as part of a mechanism regulating the relationships between the coral and its algal endosymbionts ( zooxanthellae). We envision that the effect of the proteins' fluorescence on algal physiology may be achieved not only through photosynthesis modulation, but also through regulatory photosensors analogous to phytochromes and cryptochromes of higher plants. Such a regulation would require relatively subtle, but spectrally precise, modi. cations of the light field. Evolution of such a mechanism would explain both the adaptive diversification of colors and the coevolutionary chase at the putative algae-protein binding interface in coral fluorescent proteins.
引用
收藏
页码:332 / U15
页数:13
相关论文
共 43 条
[1]   An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein [J].
Ando, R ;
Hama, H ;
Yamamoto-Hino, M ;
Mizuno, H ;
Miyawaki, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (20) :12651-12656
[2]   Accuracy and power of Bayes prediction of amino acid sites under positive selection [J].
Anisimova, M ;
Bielawski, JP ;
Yang, ZH .
MOLECULAR BIOLOGY AND EVOLUTION, 2002, 19 (06) :950-958
[3]   Corals' adaptive response to climate change [J].
Baker, AC ;
Starger, CJ ;
McClanahan, TR ;
Glynn, PW .
NATURE, 2004, 430 (7001) :741-741
[4]   Darwinian adaptation of proteorhodopsin to different light intensities in the marine environment [J].
Bielawski, JP ;
Dunn, KA ;
Sabehi, G ;
Béjà, O .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (41) :14824-14829
[5]   Applications of ancestral protein reconstruction in understanding protein function: GFP-like proteins [J].
Chang, BSW ;
Ugalde, JA ;
Matz, MV .
MOLECULAR EVOLUTION: PRODUCING THE BIOCHEMICAL DATA, PART B, 2005, 395 :652-670
[6]   Host benefit and the evolution of specialization in symbiosis [J].
Douglas, AE .
HEREDITY, 1998, 81 :599-603
[8]   Color transitions in coral's fluorescent proteins by site-directed mutagenesis [J].
Gurskaya, Nadya G. ;
Savitsky, Alexander P. ;
Yanushevich, Yurii G. ;
Lukyanov, Sergey A. ;
Lukyanov, Konstantin A. .
BMC BIOCHEMISTRY, 2001, 2
[9]   Mapping of binding sites for nidogens, fibulin-2, fibronectin and heparin to different IG modules of perlecan [J].
Hopf, M ;
Göhring, W ;
Mann, K ;
Timpl, R .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 311 (03) :529-541
[10]   Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1 [J].
Hopf, M ;
Göhring, W ;
Ries, A ;
Timpl, R ;
Hohenester, E .
NATURE STRUCTURAL BIOLOGY, 2001, 8 (07) :634-640