Detail
Článek
Článek online
FT
Medvik - BMČ
  • Je něco špatně v tomto záznamu ?

Evolution of moth sex pheromone composition by a single amino acid substitution in a fatty acid desaturase

A. Buček, P. Matoušková, H. Vogel, P. Šebesta, U. Jahn, J. Weißflog, A. Svatoš, I. Pichová,

. 2015 ; 112 (41) : 12586-91. [pub] 20150928

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc16009945
E-zdroje Online Plný text

NLK Free Medical Journals od 1915 do Před 6 měsíci
Freely Accessible Science Journals od 1915 do Před 6 měsíci
PubMed Central od 1915 do Před 6 měsíci
Europe PubMed Central od 1915 do Před 6 měsíci
Open Access Digital Library od 1915-01-01
Open Access Digital Library od 1915-01-15

Odkazy

PubMed 26417103
DOI 10.1073/pnas.1514566112
Knihovny.cz E-zdroje

For sexual communication, moths primarily use blends of fatty acid derivatives containing one or more double bonds in various positions and configurations, called sex pheromones (SPs). To study the molecular basis of novel SP component (SPC) acquisition, we used the tobacco hornworm (Manduca sexta), which uses a blend of mono-, di-, and uncommon triunsaturated fatty acid (3UFA) derivatives as SP. We identified pheromone-biosynthetic fatty acid desaturases (FADs) MsexD3, MsexD5, and MsexD6 abundantly expressed in the M. sexta female pheromone gland. Their functional characterization and in vivo application of FAD substrates indicated that MsexD3 and MsexD5 biosynthesize 3UFAs via E/Z14 desaturation from diunsaturated fatty acids produced by previously characterized Z11-desaturase/conjugase MsexD2. Site-directed mutagenesis of sequentially highly similar MsexD3 and MsexD2 demonstrated that swapping of a single amino acid in the fatty acyl substrate binding tunnel introduces E/Z14-desaturase specificity to mutated MsexD2. Reconstruction of FAD gene phylogeny indicates that MsexD3 was recruited for biosynthesis of 3UFA SPCs in M. sexta lineage via gene duplication and neofunctionalization, whereas MsexD5 representing an alternative 3UFA-producing FAD has been acquired via activation of a presumably inactive ancestral MsexD5. Our results demonstrate that a change as small as a single amino acid substitution in a FAD enzyme might result in the acquisition of new SP compounds.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc16009945
003      
CZ-PrNML
005      
20160418102911.0
007      
ta
008      
160408s2015 xxu f 000 0|eng||
009      
AR
024    7_
$a 10.1073/pnas.1514566112 $2 doi
024    7_
$a 10.1073/pnas.1514566112 $2 doi
035    __
$a (PubMed)26417103
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxu
100    1_
$a Buček, Aleš $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague 6, Czech Republic;
245    10
$a Evolution of moth sex pheromone composition by a single amino acid substitution in a fatty acid desaturase / $c A. Buček, P. Matoušková, H. Vogel, P. Šebesta, U. Jahn, J. Weißflog, A. Svatoš, I. Pichová,
520    9_
$a For sexual communication, moths primarily use blends of fatty acid derivatives containing one or more double bonds in various positions and configurations, called sex pheromones (SPs). To study the molecular basis of novel SP component (SPC) acquisition, we used the tobacco hornworm (Manduca sexta), which uses a blend of mono-, di-, and uncommon triunsaturated fatty acid (3UFA) derivatives as SP. We identified pheromone-biosynthetic fatty acid desaturases (FADs) MsexD3, MsexD5, and MsexD6 abundantly expressed in the M. sexta female pheromone gland. Their functional characterization and in vivo application of FAD substrates indicated that MsexD3 and MsexD5 biosynthesize 3UFAs via E/Z14 desaturation from diunsaturated fatty acids produced by previously characterized Z11-desaturase/conjugase MsexD2. Site-directed mutagenesis of sequentially highly similar MsexD3 and MsexD2 demonstrated that swapping of a single amino acid in the fatty acyl substrate binding tunnel introduces E/Z14-desaturase specificity to mutated MsexD2. Reconstruction of FAD gene phylogeny indicates that MsexD3 was recruited for biosynthesis of 3UFA SPCs in M. sexta lineage via gene duplication and neofunctionalization, whereas MsexD5 representing an alternative 3UFA-producing FAD has been acquired via activation of a presumably inactive ancestral MsexD5. Our results demonstrate that a change as small as a single amino acid substitution in a FAD enzyme might result in the acquisition of new SP compounds.
650    _2
$a sekvence aminokyselin $7 D000595
650    12
$a substituce aminokyselin $7 D019943
650    _2
$a zvířata $7 D000818
650    12
$a molekulární evoluce $7 D019143
650    _2
$a desaturasy mastných kyselin $x genetika $x metabolismus $7 D044943
650    _2
$a nenasycené mastné kyseliny $x genetika $x metabolismus $7 D005231
650    _2
$a ženské pohlaví $7 D005260
650    _2
$a hmyzí proteiny $x genetika $x metabolismus $7 D019476
650    _2
$a Manduca $x genetika $x metabolismus $7 D018402
650    _2
$a molekulární sekvence - údaje $7 D008969
650    _2
$a fylogeneze $7 D010802
650    _2
$a sexuální lákadla $x biosyntéza $x genetika $7 D012724
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Matoušková, Petra $u Faculty of Pharmacy, Charles University in Prague, 500 05 Hradec Králové, Czech Republic;
700    1_
$a Vogel, Heiko $u Max Planck Institute for Chemical Ecology, Department of Entomology, D-07745, Jena, Germany;
700    1_
$a Šebesta, Petr $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague 6, Czech Republic;
700    1_
$a Jahn, Ullrich $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague 6, Czech Republic;
700    1_
$a Weißflog, Jerrit $u Max Planck Institute for Chemical Ecology, Mass Spectrometry Group, D-07745, Jena, Germany.
700    1_
$a Svatoš, Aleš $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague 6, Czech Republic; Max Planck Institute for Chemical Ecology, Mass Spectrometry Group, D-07745, Jena, Germany svatos@ice.mpg.de iva.pichova@uochb.cas.cz.
700    1_
$a Pichová, Iva $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague 6, Czech Republic; svatos@ice.mpg.de iva.pichova@uochb.cas.cz.
773    0_
$w MED00010472 $t Proceedings of the National Academy of Sciences of the United States of America $x 1091-6490 $g Roč. 112, č. 41 (2015), s. 12586-91
856    41
$u https://pubmed.ncbi.nlm.nih.gov/26417103 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20160408 $b ABA008
991    __
$a 20160418102958 $b ABA008
999    __
$a ok $b bmc $g 1113374 $s 934313
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2015 $b 112 $c 41 $d 12586-91 $e 20150928 $i 1091-6490 $m Proceedings of the National Academy of Sciences of the United States of America $n Proc Natl Acad Sci U S A $x MED00010472
LZP    __
$a Pubmed-20160408

Najít záznam

Citační ukazatele

Možnosti archivace