Study on a detection method of protein tyrosine sulfation modification in zebrafish
Received date: 2022-01-23
Revised date: 2022-02-02
Online published: 2022-02-09
Supported by
Supported by the National Key Research and Development Program of China Nos(2018YFA0800200);Supported by the National Key Research and Development Program of China Nos(2018YFA0801000);the National Natural Science Foundation of China Nos(32030032);the National Natural Science Foundation of China Nos(31830061);the Strategic Priority Research Program of the Chinese Academy of Sciences, China No(XDA16010207)
Protein tyrosine sulfation (PTS) is an important post-translational modification that regulates a variety of physiological and pathological processes. However, PTS is unstable and lacks effective enrichment methods, which make it difficult to be detected in biological samples. In this study, we detected the tyrosine sulfation modification level of total proteins in developing zebrafish embryos by using high-resolution mass spectrometer, Orbitrap Exploris 480. A total of 26 proteins with tyrosine sulfation were detected, including membrane proteins, secreted proteins, cytoplasmic proteins and nucleoproteins. This study established a methodology in detecting protein tyrosine sulfation modification in embryonic zebrafish, which paved the way for evaluating the biological function of PTS.
Tingting Zhang, Feng Liu . Study on a detection method of protein tyrosine sulfation modification in zebrafish[J]. Hereditas(Beijing), 2022 , 44(2) : 178 -186 . DOI: 10.16288/j.yczz.22-018
| [1] | Moore KL. The biology and enzymology of protein tyrosine O-sulfation. J Biol Chem, 2003, 278(27):24243-24246. |
| [2] | Yang YS, Wang CC, Chen BH, Hou YH, Hung KS, Mao YC. Tyrosine sulfation as a protein post-translational modification. Molecules, 2015, 20(2):2138-2164. |
| [3] | Kaufmann C, Stührwohldt N, Sauter M. Tyrosylprotein sulfotransferase-dependent and -independent regulation of root development and signaling by PSK LRR receptor kinases in Arabidopsis. J Exp Bot, 2021, 72(15):5508-5521. |
| [4] | De Giorgi J, Fuchs C, Iwasaki M, Kim W, Piskurewicz U, Gully K, Utz-Pugin A, Mène-Saffrané L, Waridel P, Nawrath C, Longoni FP, Fujita S, Loubéry S, Lopez- Molina L. The Arabidopsis mature endosperm promotes seedling cuticle formation via release of sulfated peptides. Dev Cell, 2021, 56(22): 3066-3081.e5. |
| [5] | Kehoe JW, Bertozzi CR. Tyrosine sulfation: a modulator of extracellular protein-protein interactions. Chem Biol, 2000, 7(3):R57-R61. |
| [6] | Ludeman JP, Stone MJ. The structural role of receptor tyrosine sulfation in chemokine recognition. Br J Pharmacol, 2014, 171(5):1167-1179. |
| [7] | Farzan M, Mirzabekov T, Kolchinsky P, Wyatt R, Cayabyab M, Gerard NP, Gerard C, Sodroski J, Choe H. Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry. Cell, 1999, 96(5):667-676. |
| [8] | Seibert C, Veldkamp CT, Peterson FC, Chait BT, Volkman BF, Sakmar TP. Sequential tyrosine sulfation of CXCR4 by tyrosylprotein sulfotransferases. Biochemistry, 2008, 47(43):11251-11262. |
| [9] | Tinoco R, Otero DC, Takahashi AA, Bradley LM. PSGL-1: A new player in the immune checkpoint landscape. Trends Immunol, 2017, 38(5):323-335. |
| [10] | Pouyani T, Seed B. PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus. Cell, 1995, 83(2):333-343. |
| [11] | Westmuckett AD, Moore KL. Lack of tyrosylprotein sulfotransferase activity in hematopoietic cells drastically attenuates atherosclerosis in Ldlr -/- mice. Arterioscler Thromb Vasc Biol, 2009, 29(11):1730-1736. |
| [12] | Stone MJ, Chuang S, Hou X, Shoham M, Zhu JZ. Tyrosine sulfation: an increasingly recognised post-translational modification of secreted proteins. N Biotechnol, 2009, 25(5):299-317. |
| [13] | Stone SR, Hofsteenge J. Kinetics of the inhibition of thrombin by hirudin. Biochemistry, 1986, 25(16):4622-4628. |
| [14] | Robinson MR, Brodbelt JS. Integrating Weak Anion Exchange and Ultraviolet Photodissociation Mass Spectrometry with Strategic Modulation of Peptide Basicity for the Enrichment of Sulfopeptides. Anal Chem, 2016, 88(22):11037-11045. |
| [15] | Wu CC, MacCoss MJ, Howell KE, Yates JR. A method for the comprehensive proteomic analysis of membrane proteins. Nat Biotechnol, 2003, 21(5):532-538. |
| [16] | Nagaraj N, Lu AP, Mann M, Wiśniewski JR. Detergent-based but gel-free method allows identification of several hundred membrane proteins in single LC-MS runs. J Proteome Res, 2008, 7(11):5028-5032. |
| [17] | Blonder J, Xiao Z, Veenstra TD. Proteomic profiling of differentiating osteoblasts. Expert Rev Proteomics, 2006, 3(5):483-496. |
| [18] | Rappsilber J, Mann M, Ishihama Y. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc, 2007, 2(8):1896-1906. |
| [19] | Cao L, Wu XM, Nie P, Chang MX. The negative regulation of piscine CD44c in viral and bacterial infection. Dev Comp Immunol, 2019, 96:135-143. |
| [20] | Harty BL, Krishnan A, Sanchez NE, Schiöth HB, Monk KR. Defining the gene repertoire and spatiotemporal expression profiles of adhesion G protein-coupled receptors in zebrafish. BMC Genomics, 2015, 16(1):62. |
| [21] | Wu XJ, Thomas P, Zhu Y. Pgrmc1 knockout impairs oocyte maturation in zebrafish. Front Endocrinol (Lausanne), 2018, 9:560. |
| [22] | Yang Y, Wang L, Han X, Yang WL, Zhang MM, Ma HL, Sun BF, Li A, Xia J, Chen J, Heng J, Wu BX, Chen YS, Xu JW, Yang X, Yao H, Sun JW, Lyu C, Wang HL, Huang Y, Sun YP, Zhao YL, Meng AM, Ma JB, Liu F, Yang YG. RNA 5-methylcytosine facilitates the maternal-to-zygotic transition by preventing maternal mRNA decay. Mol Cell, 2019, 75(6): 1188-1202.e11. |
| [23] | Hodatsu A, Konno T, Hayashi K, Funada A, Fujita T, Nagata Y, Fujino N, Kawashiri MA, Yamagishi M. Compound heterozygosity deteriorates phenotypes of hypertrophic cardiomyopathy with founder MYBPC3 mutation: evidence from patients and zebrafish models. Am J Physiol Heart Circ Physiol, 2014, 307(11):H1594-H1604. |
| [24] | Grundt K, Haga IV, Huitfeldt HS, Ostvold AC. Identification and characterization of two putative nuclear localization signals (NLS) in the DNA-binding protein NUCKS. Biochim Biophys Acta, 2007, 1773(9):1398-1406. |
| [25] | Hu YW, Wu XM, Ren SS, Cao L, Nie P, Chang MX. NOD1 deficiency impairs CD44a/Lck as well as PI3K/Akt pathway. Sci Rep, 2017, 7(1):2979. |
| [26] | Chen YH, Pai CW, Huang SW, Chang SN, Lin LY, Chiang FT, Lin JL, Hwang JJ, Tsai CT. Inactivation of Myosin binding protein C homolog in zebrafish as a model for human cardiac hypertrophy and diastolic dysfunction. J Am Heart Assoc, 2013, 2(5):e000231. |
| [27] | Liu TA, Yasuda S, Williams FE, Liu MY, Suiko M, Sakakibara Y, Yang YS, Liu MC. A target-specific approach for the identification of tyrosine-sulfated hemostatic proteins. Anal Biochem, 2009, 390(1):88-90. |
| [28] | Lassen KS, Bradbury ARM, Rehfeld JF, Heegaard NHH. Microscale characterization of the binding specificity and affinity of a monoclonal antisulfotyrosyl IgG antibody. Electrophoresis, 2008, 29(12):2557-2564. |
| [29] | Zhou WB, Duckworth BP, Geraghty RJ. Fluorescent peptide sensors for tyrosylprotein sulfotransferase activity. Anal Biochem, 2014, 461:1-6. |
| [30] | Niehrs C, Huttner WB. Purification and characterization of tyrosylprotein sulfotransferase. EMBO J, 1990, 9(1):35-42. |
| [31] | Edelson-Averbukh M, Shevchenko A, Pipkorn R, Lehmann WD. Discrimination between peptide O-sulfo- and O-phosphotyrosine residues by negative ion mode electrospray tandem mass spectrometry. J Am Soc Mass Spectrom, 2011, 22(12):2256-2268. |
| [32] | Salek M, Costagliola S, Lehmann WD. Protein tyrosine- O-sulfation analysis by exhaustive product ion scanning with minimum collision offset in a NanoESI Q-TOF tandem mass spectrometer. Anal Chem, 2004, 76(17):5136-5142. |
| [33] | Nguyen J, Russell SC. Targeted proteomics approach to species-level identification of Bacillus thuringiensis spores by AP-MALDI-MS. J Am Soc Mass Spectrom, 2010, 21(6):993-1001. |
| [34] | Wiśniewski JR, Zougman A, Nagaraj N, Mann M. Universal sample preparation method for proteome analysis. Nat Methods, 2009, 6(5):359-362. |
| [35] | Wiśniewski JR, Zougman A, Mann M. Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome. J Proteome Res, 2009, 8(12):5674-5678. |
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