Abstract:The water sources in the livestock areas in the central and western parts of northern China are mostly high-salt water sources. Ordinary livestock cannot adapt to such water sources, thus affecting the development of animal husbandry in the northern regions. Bactrian camel (Camelidae bactrianus) has a species capable of adapting to high salt water source in the extreme environment of northern desert, but its adaptation mechanism is still unclear. In this study, bactrian camel's salt adaptability was concerned and bactrian camel colon tissue under salt stress conditions and normal conditions was sequenced to understand the mechanism of adaptability of camel's colon tissues to a salt stress environment. The results showed that 52 882 246 reads were measured in the test group and 51 533 346 in the control group; the total mapped rate of reads in the test group was 86.41%, the uniquely mapped rate was 84.61%, the total mapped rate of reads in the control group was 92.48%, the uniquely mapped rate was 91.62 %; 2 450 differentially expressed genes were obtained, among which 1 136 genes were up-regulated and 1 314 were down-regulated. Gene Ontology (GO) analysis results showed that there were 17 terms that had significantly down-regulated expression of genes and 28 terms that had significantly up-regulated expression of genes. There was no statistically significant enrichment term in the up-regulated expression of genes. The Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analysis showed that the down-regulated expression genes were significantly enriched to include spliceosome, RNA transport, basal transcription factors, ribosome biogenesis in eukaryotes, RNA degradation,oxidative phosphorylation and protein export; up-regulation of expression of genes were not found in enriched pathways. The above results indicated that genes with down-regulated expression in colon were more than up-regulated expressed genes in salt stress. Statistically significant biological function analysis showed that down-regulated expression genes were involved in RNA processes and protein synthesis pathways. These genes were favorable for reducing RNA synthesis and reducing the metabolic rate of colon tissue. This study analyzes the salt adaptation mechanism of regional characteristic livestock breeds, and provides salt adaptation molecular theory for breeding, thereby improving regional resource utilization.
BALLARINO M, JOBERT L, DEMB L D, et al. 2013. TAF15 is important for cellular proliferation and regulates the expression of a subset of cell cycle genes through miRNAs. Oncogene [J], 32: 4646-4655.BEN Y S, DIX I, RUSSELL C S, et al. 1998. Identification and functional analysis of hPRP17, the human homologue of the PRP17/CDC40 yeast gene involved in splicing and cell cycle control. Rna-a Publication of the Rna Society [J], 4: 1304.BUSS F, STEWART M 1995. Macromolecular Interactions in the Nucleoporin p62 Complex of Rat Nuclear Pores: Binding of Nucleoporin p54 to the Rod Domain of p62. Journal of Cell Biology [J], 128: 251-261.CHALKLEY G E, VERRIJZER C P 1999. DNA binding site selection by RNA polymerase II TAFs: a TAF(II)250-TAF(II)150 complex recognizes the initiator. Embo Journal [J], 18: 4835-4845.CHUANG T W, LEE K M, LOU Y C, et al. 2016. A Point Mutation in the Exon Junction Complex Factor Y14 Disrupts Its Function in mRNA Cap Binding and Translation Enhancement. Journal of Biological Chemistry [J], 291: 8565.CLER E, PAPAI G, SCHULTZ P, et al. 2009. Recent advances in understanding the structure and function of general transcription factor TFIID. Cellular and Molecular Life Sciences [J], 66: 2123-2134.D G, L H, J B, et al. 2001. Bms1p, a novel GTP-binding protein, and the related Tsr1p are required for distinct steps of 40S ribosome biogenesis in yeast. Rna-a Publication of the Rna Society [J], 7: 1268.DEJGAARD K, THEBERGE J F, HEATH-ENGEL H, et al. 2010. Organization of the Sec61 translocon, studied by high resolution native electrophoresis. Journal of Proteome Research [J], 9: 1763-1771.EBMEIER C C, ERICKSON B, ALLEN B L, et al. 2017. Human TFIIH kinase CDK7 regulates transcription-associated chromatin modifications. Cell Reports [J], 20: 1173.FETZER S, LAUBER J, WILL C L, et al. 1997. The [U4/U6.U5] tri-snRNP-specific 27K protein is a novel SR protein that can be phosphorylated by the snRNP-associated protein kinase. RNA [J], 3: 344.FREED E F, BLEICHERT F, DUTCA L M, et al. 2010. When ribosomes go bad: diseases of ribosome biogenesis. Molecular BioSystems [J], 6: 481-493.GONZ LEZAGUILERA C, ASKJAER P 2012. Dissecting the NUP107 complex: multiple components and even more functions. Nucleus [J], 3: 340-348.GRUNDHOFF A T, KREMMER E, T RECI O, et al. 1999. Characterization of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C. Journal of Biological Chemistry [J], 274: 19136-19144.HARTUNG S, HOPFNER K P 2007. The exosome, plugged. EMBO reports [J], 8: 456-457.HINCHLIFFE P, CARROLL J, SAZANOV L A 2006. Identification of a Novel Subunit of Respiratory Complex I from Thermus thermophilus. Biochemistry [J], 45: 4413-4420.HOUSELEY J, TOLLERVEY D 2009. The Many Pathways of RNA Degradation. Cell [J], 136: 763-776.HUBER J T, GILLASPY M L 2000. National Cancer Institute (NCI). Encyclopedic Dictionary of AIDS-Related Terminology [J].IAKHIAEVA E, IAKHIAEV A, ZWIEB C 2010. Identification of amino acid residues in protein SRP72 required for binding to a kinked 5e motif of the human signal recognition particle RNA. Bmc Molecular Biology [J], 11: 83.IAKHIAEVA E, WOWER J, WOWER I K, et al. 2008. The 5e motif of eukaryotic signal recognition particle RNA contains a conserved adenosine for the binding of SRP72. Rna-a Publication of the Rna Society [J], 14: 1143-1153.ISHIGAKI Y, NAKAMURA Y, TATSUNO T, et al. 2013. Depletion of RNA-binding protein RBM8A (Y14) causes cell cycle deficiency and apoptosis in human cells. Experimental Biology & Medicine [J], 238: 889-897.JAGOTLACOUSSIERE L, FAYE A, BRUZZONIGIOVANELLI H, et al. 2015. DNA damage-induced nuclear translocation of Apaf-1 is mediated by nucleoporin Nup107. Cell Cycle [J], 14: 1242-1251.KATHARINA B, KATJA W, KARL‐PETER H 2006. The exosome: a macromolecular cage for controlled RNA degradation. Molecular Microbiology [J], 61: 1372-1379.KRESSLER D, HURT E, BASSLER J 2010. Driving ribosome assembly. Biochimica Et Biophysica Acta [J], 1803: 673-683.LAVIGNE A C, MENGUS G, MAY M, et al. 1996. Multiple interactions between hTAFII55 and other TFIID subunits. Requirements for the formation of stable ternary complexes between hTAFII55 and the TATA-binding protein. Journal of Biological Chemistry [J], 271: 19774-19780.LI B, LI Y M, HE W T, et al. 2016. Knockdown of DDX46 inhibits proliferation and induces apoptosis in esophageal squamous cell carcinoma cells. Oncology Reports [J], 36: 223.LINDSEY L A, GARCIABLANCO M A 1998. Functional conservation of the human homolog of the yeast pre-mRNA splicing factor Prp17p. Journal of Biological Chemistry [J], 273: 32771-32775.LIU S, RAUHUT R, VORNLOCHER H, et al. 2006. The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP. Rna-a Publication of the Rna Society [J], 12: 1418.M B, C L, V M, et al. 1999. Three-dimensional structures of the TAFII-containing complexes TFIID and TFTC. Science [J], 286: 2151-2153.MALIK S, ROEDER R G 2000. Transcriptional regulation through Mediator-like coactivators in yeast and metazoan cells. Trends in Biochemical Sciences [J], 25: 277-283.MARTINEZ E 2002. Multi-protein complexes in eukaryotic gene transcription. Plant Molecular Biology [J], 50: 925-947.MAZZA C, OHNO M, SEGREF A, et al. 2001. Crystal Structure of the Human Nuclear Cap Binding Complex. Molecular Cell [J], 8: 383-396.MAZZA C, SEGREF A, MATTAJ I W, et al. 2014. Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex. Embo Journal [J], 21: 5548-5557.MURPHY J M, HANSEN D S 2009. Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays. Journal of Molecular Biology [J], 393: 409-424.N S? N-HERN? N, S B, U S, et al. 2016. The in vivo dynamics of TCERG1, a factor that couples transcriptional elongation with splicing. Rna-a Publication of the Rna Society [J], 22: 571-582.NG S Y, CHABAN B, VANDYKE D J, et al. 2007. Archaeal signal peptidases. Microbiology [J], 153: 305-314.NILSON K, GUO J, TUREK M, et al. 2015. THZ1 Reveals Roles for Cdk7 in Co-transcriptional Capping and Pausing. Molecular Cell [J], 59: 576-587.PABIS M, NEUFELD N, SHAV-TAL Y, et al. 2010. Binding properties and dynamic localization of an alternative isoform of the cap-binding complex subunit CBP20. Nucleus [J], 1: 412-421.PALANCADE, BENO T, DOYE, et al. 2008. Sumoylating and desumoylating enzymes at nuclear pores: underpinning their unexpected duties? Trends in Cell Biology [J], 18: 174-183.PINTO A L, STEITZ J A 1989. The mammalian analogue of the yeast PRP8 splicing protein is present in the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome. Proceedings of the National Academy of Sciences of the United States of America [J], 86: 8742-8746.RITCHIE D B, SCHELLENBERG M J, MACMILLAN A M 2009. Spliceosome structure: Piece by piece. Biochimica Et Biophysica Acta [J], 1789: 624-633.SAZANOV L A, HINCHLIFFE P 2006. Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus. Science [J], 311: 1430-1436.SHIN E M, HUI S H, LEE M H, et al. 2014. DEAD-box helicase DP103 defines metastatic potential of human breast cancers. Journal of Clinical Investigation [J], 124: 3807.SOKHI U K, BACOLOD M D, EMDAD L, et al. 2014. Analysis of global changes in gene expression induced by human polynucleotide phosphorylase (hPNPaseold-35). Journal of Cellular Physiology [J], 229: 1952–1962.SOLARI S, BAKER R J 2006. Mammal Species of the World: A Taxonomic and Geographic Reference by D. E. Wilson; D. M. Reeder. Mastozoología Neotropical [J], 13: 290-293.STEVENS R 2010. Gray's Anatomy for Students [M]. 北京大学医学出版社.SUH J L, WATTS B, STUCKEY J I, et al. 2018. Quantitative characterization of bivalent probes for a dual bromodomain protein, Transcription Initiation Factor TFIID subunit 1, TAF1. Biochemistry [J], 57.SUZUKI T, IZUMI H, OHNO M 2010. Cajal body surveillance of U snRNA export complex assembly. The Journal of Cell Biology [J], 190: 603-612.TAWAMIE H, MARTIANOV I, WOHLFAHRT N, et al. 2017. Hypomorphic Pathogenic Variants in TAF13 Are Associated with Autosomal-Recessive Intellectual Disability and Microcephaly. American Journal of Human Genetics [J], 100: 555.THOMAS F, KUTAY U 2003. Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway. Journal of Cell Science [J], 116: 2409-2419.WAHL M, WILL C, LUHRMANN R 2009. The Spliceosome: Design Principles of a Dynamic RNP Machine. Cell [J], 136: 701-718.WANG Y, ZHANG T, KWIATKOWSKI N, et al. 2015. CDK7-dependent transcriptional addiction in triple-negative breast cancer. Cell [J], 163: 174-186.YZ X, CM N, S K, et al. 2014. Prp5 bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA. The EMBO Journal [J], 23: 376-385.ZHANG X, YANG H, CORYDON M J, et al. 1999. Localization of a Human Nucleoporin 155 Gene (NUP155) to the 5p13 Region and Cloning of Its cDNA. Genomics [J], 57: 144-151.ZHOU Z, REED R 2014. Human homologs of yeast Prp16 and Prp17 reveal conservation of the mechanism for catalytic step II of pre-mRNA splicing. Embo Journal [J], 17: 2095-2106.