Insights on the evolution of trehalose biosynthesis

被引:386
作者
Avonce, Nelson
Mendoza-Vargas, Alfredo
Morett, Enrique
Iturriaga, Gabriel
机构
[1] Univ Nacl Autonoma Mexico, Inst Biotecnol, Cuernavaca 62210, Morelos, Mexico
[2] UAEM, Ctr Invest Biotecnol, Cuernavaca 62210, Morelos, Mexico
关键词
D O I
10.1186/1471-2148-6-109
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Background: The compatible solute trehalose is a non-reducing disaccharide, which accumulates upon heat, cold or osmotic stress. It was commonly accepted that trehalose is only present in extremophiles or cryptobiotic organisms. However, in recent years it has been shown that although higher plants do not accumulate trehalose at significant levels they have actively transcribed genes encoding the corresponding biosynthetic enzymes. Results: In this study we show that trehalose biosynthesis ability is present in eubacteria, archaea, plants, fungi and animals. In bacteria there are five different biosynthetic routes, whereas in fungi, plants and animals there is only one. We present phylogenetic analyses of the trehalose-6-phosphate synthase (TPS) and trehalose-phosphatase (TPP) domains and show that there is a close evolutionary relationship between these domains in proteins from diverse organisms. In bacteria TPS and TPP genes are clustered, whereas in eukaryotes these domains are fused in a single protein. Conclusion: We have demonstrated that trehalose biosynthesis pathways are widely distributed in nature. Interestingly, several eubacterial species have multiple pathways, while eukaryotes have only the TPS/TPP pathway. Vertebrates lack trehalose biosynthetic capacity but can catabolise it. TPS and TPP domains have evolved mainly in parallel and it is likely that they have experienced several instances of gene duplication and lateral gene transfer.
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页数:15
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共 67 条
[1]   BASIC LOCAL ALIGNMENT SEARCH TOOL [J].
ALTSCHUL, SF ;
GISH, W ;
MILLER, W ;
MYERS, EW ;
LIPMAN, DJ .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 215 (03) :403-410
[2]   Physiological roles of trehalose in bacteria and yeasts:: a comparative analysis [J].
Argüelles, JC .
ARCHIVES OF MICROBIOLOGY, 2000, 174 (04) :217-224
[3]   Trehalose metabolism and glucose sensing in plants [J].
Avonce, N ;
Leyman, B ;
Thevelein, J ;
Iturriaga, G .
BIOCHEMICAL SOCIETY TRANSACTIONS, 2005, 33 :276-279
[4]   The Arabidopsis trehalose-6-P synthase AtTPS1 gene is a regulator of glucose, abscisic acid, and stress signaling [J].
Avonce, N ;
Leyman, B ;
Mascorro-Gallardo, JO ;
Van Dijck, P ;
Thevelein, JM ;
Iturriaga, G .
PLANT PHYSIOLOGY, 2004, 136 (03) :3649-3659
[5]   The regulation of trehalose metabolism in insects [J].
Becker, A ;
Schloder, P ;
Steele, JE ;
Wegener, G .
EXPERIENTIA, 1996, 52 (05) :433-439
[6]   Composition and functional analysis of the Saccharomyces cerevisiae trehalose synthase complex [J].
Bell, W ;
Sun, WN ;
Hohmann, S ;
Wera, S ;
Reinders, A ;
De Virgilio, C ;
Wiemken, A ;
Thevelein, JM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (50) :33311-33319
[7]   Isolation and molecular characterization of the Arabidopsis TPS1 gene, encoding trehalose-6-phosphate synthase [J].
Blázquez, MA ;
Santos, E ;
Flores, CL ;
Martínez-Zapater, JM ;
Salinas, J ;
Gancedo, C .
PLANT JOURNAL, 1998, 13 (05) :685-689
[8]  
CABIB E, 1958, J BIOL CHEM, V231, P259
[9]   Evolution and function of the sucrose-phosphate synthase gene families in wheat and other grasses [J].
Castleden, CK ;
Aoki, N ;
Gillespie, VJ ;
MacRae, EA ;
Quick, WP ;
Buchner, P ;
Foyer, CH ;
Furbank, RT ;
Lunn, JE .
PLANT PHYSIOLOGY, 2004, 135 (03) :1753-1764
[10]   Obcells as proto-organisms: Membrane heredity, lithophosphorylation, and the origins of the genetic code, the first cells, and photosynthesis [J].
Cavalier-Smith, T .
JOURNAL OF MOLECULAR EVOLUTION, 2001, 53 (4-5) :555-595