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1.
Genomics ; 104(6 Pt B): 572-81, 2014 Dec.
Article in English | MEDLINE | ID: mdl-25304740

ABSTRACT

Changing bovine milk fatty acid (FA) composition through selection can decrease saturated FA (SFA) consumption, improve human health and provide a means for manipulating processing properties of milk. Our study determined associations between milk FA composition and genes from triacylglycerol (TAG) biosynthesis pathway. The GC dinucleotide allele of diacylglycerol O-acyltransferase 1:g.10433-10434AA >GC was associated with lower palmitic acid (16:0) concentration but higher oleic (18:1 cis-9), linoleic (18:2 cis-9, cis-12) acid concentrations, and elongation index. Accordingly, the GC dinucleotide allele was associated with lower milk fat percentage and SFA concentrations but higher monounsaturated FA and polyunsaturated FA (PUFA) concentrations. The glycerol-3-phosphate acyltransferase, mitochondrial haplotypes were associated with higher myristoleic acid (14:1 cis-9) concentration and C14 desaturation index. The 1-acylglycerol-3-phosphate acyltransferase 1 haplotypes were associated with higher PUFA and linoleic acid concentrations. The results of this study provide information for developing genetic tools to modify milk FA composition in dairy cattle.


Subject(s)
Cattle/genetics , Diacylglycerol O-Acyltransferase/genetics , Fatty Acids/analysis , Glycerol-3-Phosphate O-Acyltransferase/genetics , Milk/chemistry , Polymorphism, Single Nucleotide , Animals , Lipogenesis/genetics
2.
Dev Dyn ; 239(6): 1849-57, 2010 Jun.
Article in English | MEDLINE | ID: mdl-20503380

ABSTRACT

The CD133/prominin1 gene encodes a pentamembrane glycoprotein cell surface marker that is expressed in stem cells from neuroepithelial, hematopoietic, and various organ tissues. Here we report the analysis of two zebrafish CD133/prominin1 orthologues, prominin1a and prominin1b. The expression patterns of the zebrafish prominin1a and b genes were analyzed during embryogenesis using whole mount in situ hybridization. prominin1a and b show novel complementary and overlapping patterns of expression in proliferating zones in the developing sensory organs and central nervous system. The expression patterns suggest functional conservation of the zebrafish prominin1 genes. Initial analyses of prominin1a and b in neoplastic tissue show increased expression of both genes in a subpopulation of cells in malignant peripheral nerve sheath tumors in tp53 mutants. Based on these analyses, the zebrafish prominin1 genes will be useful markers for examining proliferating cell populations in adult organs, tissues, and tumors.


Subject(s)
Cell Proliferation , Central Nervous System/embryology , Central Nervous System/metabolism , Zebrafish/embryology , Zebrafish/genetics , AC133 Antigen , Animals , Antigens, CD , Embryo, Nonmammalian , Embryonic Development/genetics , Genes , Glycoproteins , Peptides , Sense Organs/metabolism , Zebrafish/metabolism
3.
Nat Struct Mol Biol ; 21(5): 456-63, 2014 May.
Article in English | MEDLINE | ID: mdl-24747941

ABSTRACT

CLC-type exchangers mediate transmembrane Cl(-) transport. Mutations altering their gating properties cause numerous genetic disorders. However, their transport mechanism remains poorly understood. In conventional models, two gates alternatively expose substrates to the intra- or extracellular solutions. A glutamate was identified as the only gate in the CLCs, suggesting that CLCs function by a nonconventional mechanism. Here we show that transport in CLC-ec1, a prokaryotic homolog, is inhibited by cross-links constraining movement of helix O far from the transport pathway. Cross-linked CLC-ec1 adopts a wild-type-like structure, indicating stabilization of a native conformation. Movements of helix O are transduced to the ion pathway via a direct contact between its C terminus and a tyrosine that is a constitutive element of the second gate of CLC transporters. Therefore, the CLC exchangers have two gates that are coupled through conformational rearrangements outside the ion pathway.


Subject(s)
Chloride Channels/chemistry , Escherichia coli Proteins/chemistry , Biological Transport/physiology , Chloride Channels/genetics , Chloride Channels/physiology , Crystallography, X-Ray , Escherichia coli K12/metabolism , Escherichia coli Proteins/genetics , Escherichia coli Proteins/physiology , Models, Molecular , Mutation , Protein Structure, Tertiary
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