PMID- 24330521
OWN - NLM
STAT- MEDLINE
DCOM- 20140219
LR  - 20211021
IS  - 1471-2148 (Electronic)
IS  - 1471-2148 (Linking)
VI  - 13
DP  - 2013 Dec 12
TI  - Diversity and history of the long-chain acyl-CoA synthetase (Acsl) gene family in 
      vertebrates.
PG  - 271
LID - 10.1186/1471-2148-13-271 [doi]
AB  - BACKGROUND: Fatty acids, a considerable fraction of lipid molecules, participate 
      in fundamental physiological processes. They undergo activation into their 
      corresponding CoA esters for oxidation or esterification into complex lipids 
      (e.g. triglycerides, phospholipids and cholesterol esters), a process that is 
      carried out by acyl-CoA synthases (ACS). Here we analyze the evolution of the 
      gene family encoding for the long-chain acyl-CoA synthetases (Acsl) in 
      vertebrates. RESULTS: By means of phylogenetics and comparative genomics we show 
      that genome duplications (2R) generated the diversity of Acsl genes in extant 
      vertebrate lineages. In the vertebrate ancestor two separate genes originated the 
      current Acsl1/5/6 and the Acsl3/4 gene families, and the extra gene duplicates in 
      teleosts are a consequence of the teleost specific third round of genome 
      duplication (3R). Moreover, the diversity of Acsl family members is broader than 
      anticipated. Our strategy uncovered a novel uncharacterized Acsl-like gene found 
      in teleosts, spotted gar, coelacanth and possibly lamprey, which we designate 
      Acsl2. The detailed analysis of the Acsl2 teleost gene locus strongly supports 
      the conclusion that it corresponds to a retained 2R paralogue, lost in tetrapods. 
      CONCLUSIONS: We provide here the first evolutionary analysis of the Acsl gene 
      family in vertebrates, showing the specific contribution of 2R/3R to the 
      diversity of this gene family. We find also that the division of ACSL enzymes 
      into two groups predates at least the emergence of deuterostomes. Our study 
      indicates that genome duplications significantly contributed to the elaboration 
      of fatty acid activation metabolism in vertebrates.
FAU - Lopes-Marques, Monica
AU  - Lopes-Marques M
FAU - Cunha, Isabel
AU  - Cunha I
FAU - Reis-Henriques, Maria Armanda
AU  - Reis-Henriques MA
FAU - Santos, Miguel M
AU  - Santos MM
FAU - Castro, L Filipe C
AU  - Castro LF
AD  - CIIMAR - Interdisciplinary Centre of Marine and Environmental Research, CIMAR 
      Associate Laboratory, UPorto, University of Porto, Porto, Portugal. 
      filipe.castro@ciimar.up.pt.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20131212
PL  - England
TA  - BMC Evol Biol
JT  - BMC evolutionary biology
JID - 100966975
RN  - 0 (Fatty Acids)
RN  - EC 6.2.1.- (Coenzyme A Ligases)
RN  - EC 6.2.1.3 (long-chain-fatty-acid-CoA ligase)
SB  - IM
MH  - Animals
MH  - Coenzyme A Ligases/*genetics
MH  - *Evolution, Molecular
MH  - Fatty Acids/metabolism
MH  - Fishes/genetics/metabolism
MH  - Genomics
MH  - Humans
MH  - Oxidation-Reduction
MH  - Phylogeny
MH  - Vertebrates/*genetics/metabolism
PMC - PMC3890633
EDAT- 2013/12/18 06:00
MHDA- 2014/02/20 06:00
PMCR- 2013/12/12
CRDT- 2013/12/17 06:00
PHST- 2012/12/19 00:00 [received]
PHST- 2013/12/04 00:00 [accepted]
PHST- 2013/12/17 06:00 [entrez]
PHST- 2013/12/18 06:00 [pubmed]
PHST- 2014/02/20 06:00 [medline]
PHST- 2013/12/12 00:00 [pmc-release]
AID - 1471-2148-13-271 [pii]
AID - 10.1186/1471-2148-13-271 [doi]
PST - epublish
SO  - BMC Evol Biol. 2013 Dec 12;13:271. doi: 10.1186/1471-2148-13-271.