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Intron gain and loss are rare events in vertebrates; however, comparative genome analysis of elephant sharks, tetrapods, and teleosts revealed a higher level of intron turnover in teleosts. slc26a1 and slc26a2 are members of the anion-exchanger gene family. Human, zebrafish, and Japanese pufferfish slc26a1 consist of two, two, and seven exons, respectively, and slc26a2, two, three, and four exons, respectively. To better understand intron turnover in teleosts, we analyzed the exon-intron organization of slc26a1 and slc26a2 in 81 vertebrates, including 62 ray-finned fish. In most Eurypterygii, which comprise the majority of the Neoteleostei and include Acanthomorpha, Aulopiformes, and Myctophiformes, slc26a1 and slc26a2 have seven and four exons, respectively, whereas those of most other ray-finned fishes consist of two and three exons, respectively, suggesting that intron gain occurred in both slc26a1 and slc26a2 of the Eurypterygii ancestor. In addition, notothenioid slc26a2 has six exons, suggesting that two introns were inserted into the notothenioid ancestor. The two newly acquired introns in the notothenioid consist of transposon-like sequences, suggesting that they were generated via transposon insertion. The positions of some of the newly acquired introns of slc26a1 and slc26a2 in Eurypterygii are identical or very close to those of other slc26 members. These results demonstrate the lineage-specific intron gains of slc26a1 and slc26a2 in ray-finned fish and convergence at the insertion sites of some of the newly acquired introns.
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http://dx.doi.org/10.1038/s41598-025-15147-w | DOI Listing |
Sci Rep
August 2025
School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Intron gain and loss are rare events in vertebrates; however, comparative genome analysis of elephant sharks, tetrapods, and teleosts revealed a higher level of intron turnover in teleosts. slc26a1 and slc26a2 are members of the anion-exchanger gene family. Human, zebrafish, and Japanese pufferfish slc26a1 consist of two, two, and seven exons, respectively, and slc26a2, two, three, and four exons, respectively.
View Article and Find Full Text PDFPhysiol Rep
June 2024
School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Solute carrier family 26 (Slc26) is a family of anion exchangers with 11 members in mammals (named Slc26a1-a11). Here, we identified a novel member of the slc26 family, slc26a12, located in tandem with slc26a2 in the genomes of several vertebrate lineages. BLAST and synteny analyses of various jawed vertebrate genome databases revealed that slc26a12 is present in coelacanths, amphibians, reptiles, and birds but not in cartilaginous fishes, lungfish, mammals, or ray-finned fishes.
View Article and Find Full Text PDFCompr Physiol
March 2019
Hannover Medical School, Department of Gastroenterology, Hannover, Germany.
SLC26 family members are multifunctional transporters of small anions, including Cl , HCO , sulfate, oxalate, and formate. Most SLC26 isoforms act as secondary (coupled) anion transporters, while others mediate uncoupled electrogenic transport resembling Cl channels. Of the 11 described SLC26 isoforms, the SLC26A1,2,3,6,7,9,11 are expressed in the gastrointestinal tract, where they participate in salt and water transport, surface pH-microclimate regulation, affect the microbiome composition, the absorption, and secretion of oxalate and sulfate, and other functions that require further study.
View Article and Find Full Text PDFBiochem Cell Biol
June 2019
a Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.
The human solute carrier 26 (SLC26) gene family of anion transporters consists of 10 members (-, being a pseudogene) that encode membrane glycoproteins with 14 transmembrane segments and a C-terminal cytoplasmic sulfate transporter anti-sigma antagonist domain. Thus far, mutations in eight members of the family (-, , and ) have been linked to diseases in humans. Our goal is to characterize the role of N-glycosylation and the effect of mutations in SLC26A2 and A3 proteins on their functional expression in transfected HEK-293 cells.
View Article and Find Full Text PDFBiochim Biophys Acta Biomembr
December 2017
Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada. Electronic address:
The availability of the first crystal structure of a bacterial member (SLC26Dg) of the solute carrier SLC26 family of anion transporters has allowed us to create 3-dimensional models of all 10 human members (SLC26A1-A11, A10 being a pseudogene) of these membrane proteins using the Phyre2 bioinformatic tool. The homology modeling predicted that the SLC26 human proteins, like the SLC26Dg template, all consist of 14 transmembrane segments (TM) arranged in a 7+7 inverted topology with the amino-termini of two half-helices (TM3 and 10) facing each other in the centre of the protein to create the anion-binding site, linked to a C-terminal cytosolic sulfate transporter anti-sigma factor antagonist (STAS) domain. A plethora of human diseases are associated with mutations in the genes encoding human SLC26 transporters, including chondrodysplasias with varying severity in SLC26A2 (~50 mutations, 27 point mutations), congenital chloride-losing diarrhea in SLC26A3 (~70 mutations, 31 point mutations) and Pendred Syndrome or deafness autosomal recessive type 4 in SLC26A4 (~500 mutations, 203 point mutations).
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