Clustering and Differentiation of glr-3 Gene Function and Its Homologous Proteins

Updata:01-01-1970

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DOI: https://doi.org/10.30564/jzr.v3i3.3337

Abstract:
In order to adapt to the low temperature environment, organisms transmit
excitement to the central system through the thermal sensing system, which
is a classic reflex reaction. The cold receptor GLR-3 perceives cold and pro
duces cold avoidance behavior through peripheral sensory neurons ASER.
In order to further understand the gene encoding of the cold sensing glr-3
gene and the evolution of its homologous gene group function and protein
function, the nucleotide sequence and amino acid sequence of the glr-3
gene and its homologous gene in 24 species were obtained and compared.
By clustering with the GRIK2 gene sequence of Rana chensinensis, the bio
informatics method was used to predict and sequence analyze the change of
gene, evolution rate, physical and chemical properties of protein, glycosyla
tion sites, phosphorylation sites, secondary structure and tertiary structure
of protein. The analysis results show that the glr-3 gene and its homologous
gene have obvious positive selection effect. The protein prediction analysis
showed that the glr-3 gene and its homologous genes encoded proteins
in these 25 species were hydrophilic proteins, and the proportion of side
chains of aliphatic amino acids was high. The transmembrane helix was
widespread and there were more N-glycosylation sites and O-glycosylation
sites. The protein phosphorylation sites encoded were serine, threonine and
tyrosine phosphorylation sites. Secondary structure prediction showed that
the secondary structure units of the encoded protein were α-helix, β-turn,
random coil and extended chain, and the proportion of α-helix was the larg
est. This study provides useful information on the evolution and function of
the cold sensing gene glr-3 and its homologous genes.
References:

[1] Wang Dong-feng.The effect of temperature on animals[J]. Technical Advisor for Animal Husbandry,2010,(07):24. [2] Liu Li-li,Chu Qin,Xu Qing,et al.Research progress on animal cold stress[J].Journal of Anhui Agricultural Sciences,2012,40(16):8937-8940. [3] Liu Yang.The effect of cold stimulation and rewarming on related neurobehavioral in mice[D].Heilongjiang Bayi Land Reclamation University,2019. [4] Liu Mei,Wang Xiao-yi,Dong Xin-xing,et al. Research progress on the effect of cold stress on mammalian neuroendocrine system[J].Journal of Animal Husbandry and Veterinary Medicine,2020,39(05):52-56. [5] Buijs Tamara Joëlle,McNaughton Peter Anthony.The Role of Cold-Sensitive Ion Channels in Peripheral Thermosensation[J].Front Cell Neurosci,2020,14:262. [6] Caixia Gong,Zhenhuan Ouyang,Weiqiao Zhao,et al.A Neuronal Pathway that Commands Deceleration in Drosophila Larval Light-Avoidance[J].Neurosci Bull,2019,35(6):959-968. [7] Koki Fukuhara,Richard Kvetnansky,Giovanni Cizza,et al.Interrelations between Sympathoadrenal System and Hypothalamo‐Pituitary‐Adrenocortical/Thyroid Systemsin Rats Exposed to Cold Stress[J].J Neuroendocrinol,1996,8(7):533-41. [8] Xie J.,Nagle G.T.,Ritchie A.K.,et al.Cold Stress and Corticotropin-Releasing Hormone Induced Changes in Messenger Ribonucleic Acid for the α1-Subunit of the L-Type Ca2+ Channel in the Rat Anterior Pituitary and Enriched Populations of Corticotropes[J].Neuroendocrinology,1999,70(1):10-9. [9] Ajay Dhaka,Amber N.Murray,Jayanti Mathur,et al. Petrus,Ardem Patapoutian. TRPM8 Is Required for Cold Sensation in Mice[J].Neuron,2007,54(3):371-378. [10] Juricic,María de los Ángeles,Miserey-Lenkei,et al.Non-conventional Axonal Organelles Control TRPM8 Ion Channel Trafficking and Peripheral Cold Sensing[J].Cell Rep,2020,30(13):4505-4517. [11] Ying Yin,Mengyu Wu,Lejla Zubcevic,et al.Lander and Seok-Yong Lee.Structure of the cold-and menthol-sensing ion channel TRPM8[J]. Science,2018,359(6372):237–241. [12] Shilong Yang, Xiancui Lu, Yunfei Wang,et al.A paradigm of thermal adaptation in penguins and elephants by tuning cold activation in TRPM8[D].Proc Natl Acad Sci U S A,2020 117(15):8633-8638. [13] Andrea M. Peier,Aziz Moqrich,Anne C. Hergarden,et al.A TRP Channel that Senses Cold Stimuli and Menthol[J].Cell,2002,108(5):705-715. [14] Ordás Purificación,HernándezOrtego Pablo,Vara Hugo,et al.Expression of the cold thermoreceptor TRPM8 in rodent brain thermoregulatory circuits[D].J Comp Neurol,2021,529(1):234-256. [15] Brockie P J,Madsen D M,Zheng Y,et al.Differential expression of glutamate receptor subunits in the nervous system of Caenorhabditis elegans and their regulation by the homeodomain protein UNC-42[J].J Neurosci,2001,21(5):1510-22. [16] Hiroshi Suzuki,Tod R. Thiele,Serge Faumont,et al.Functional asymmetry in Caenorhabditis elegans taste neurons and its computational role in chemotaxis[J].Nature,2008,454(7200):114-117. [17] Jianke Gong,Jinzhi Liu,Elizabeth A. Ronan,et al.A Cold-Sensing Receptor Encoded by a Glutamate Receptor Gene[J].Cell,2019,178(6):1375-1386. [18] He Jin-Jiao,Liu Yang-yang,Mao Xue-fei,et al.Bioinformatics analysis of the structure and function of SARSCoV-2 S protein[J/OL].Genomics and Applied Biology,2020. [19] Li Ji.Study on the prediction of membrane protein transmembrane helix[D].Shanghai Jiaotong University,2012. [20] Guo Ling-hui,Wang Yi,Jiang Lu,et al.Research progress on the function of exosomal membrane proteins[J].World Science and Technology-Modernization of Traditional Chinese Medicine,2021. [21] Yang ZihSyuan,Huang SzuWei,Wang WenHung,et al.Identification of Important N-Linked Glycosylation Sites in the Hemagglutinin Protein and Their Functional Impact on DC-SIGN Mediated Avian Influenza H5N1 Infection[J].Int J Mol Sci,2021,22(2):743-743. [22] Li Xiao-ying.Preliminary Study on Ginseng Proteomics,Peptidomics and Glycosylation Modification[D].Jilin University,2020. [23] Zang Xiao-ying,Fu Qiao-juan,Zhao Fu-kang,et al.Bioinformatics analysis of transcription factors related to hybrid orchid leaf color[J/OL].Molecular Plant Breeding,2021. [24] Liu Gang,Li Qing-yue,Wang Chong,et al.Molecular evolution analysis of avian SLC2A4 gene and its encoded protein GLUT4[J].The Journal of Biology,2020,37(2):29-32. [25] Chen Sha-sha.Topological modeling of protein structure and its application research[D].Suzhou University,2012. [26] Mendes Fábio K,Vanderpool Dan,Fulton Ben,et al.CAFE 5 models variation in evolutionary rates among gene families[J].Bioinformatics,2020. [27] Wang Xue-feng,Wang Wang-jian.GLUT4 Research Progress[J].Foreign Medicine·Physiology,Pathology and Clinical Medicine),2003,23(6):602 -604. [28] Zhang Nan,Zhao Ying. Regulatory mechanism of glucose transporter GLUT4 expression [J]. Chinese Journal of Biochemistry and Molecular Biology,2016,32(3):237-244. [29] Chen ChiWei,Huang LanYing,Liao ChiaFeng,et al.GasPhos:Protein Phosphorylation Site Prediction Using a New Feature Selection Approach with a GA-Aided Ant Colony System.Int J Mol Sci,2020,21(21):7891. [30] Jia Meng-wen.The correlation between mRNA sequence, structure, energy and protein secondary structure[D].Inner Mongolia University,2004.

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