Target site specificity and in vivo complexity of the mammalian arginylome
Protein arginylation mediated by arginyltransferase ATE1 is a key regulatory process essential for mammalian embryogenesis, cell migration, and protein regulation. Despite decades of studies, very little is known about the specificity of ATE1-mediated target site recognition. Here, we used in vitro...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Springer Science and Business Media LLC
2021
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| Online Access: | https://hdl.handle.net/1721.1/129727 |
| _version_ | 1826215125346942976 |
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| author | Wang, Junling Pejaver, Vikas Rao Dann, Geoffrey P. Wolf, Maxim Y. Kellis, Manolis Huang, Yun Garcia, Benjamin A. Radivojac, Predrag Kashina, Anna |
| author2 | Massachusetts Institute of Technology. Computer Science and Artificial Intelligence Laboratory |
| author_facet | Massachusetts Institute of Technology. Computer Science and Artificial Intelligence Laboratory Wang, Junling Pejaver, Vikas Rao Dann, Geoffrey P. Wolf, Maxim Y. Kellis, Manolis Huang, Yun Garcia, Benjamin A. Radivojac, Predrag Kashina, Anna |
| author_sort | Wang, Junling |
| collection | MIT |
| description | Protein arginylation mediated by arginyltransferase ATE1 is a key regulatory process essential for mammalian embryogenesis, cell migration, and protein regulation. Despite decades of studies, very little is known about the specificity of ATE1-mediated target site recognition. Here, we used in vitro assays and computational analysis to dissect target site specificity of mouse arginyltransferases and gain insights into the complexity of the mammalian arginylome. We found that the four ATE1 isoforms have different, only partially overlapping target site specificity that includes more variability in the target residues than previously believed. Based on all the available data, we generated an algorithm for identifying potential arginylation consensus motif and used this algorithm for global prediction of proteins arginylated in vivo on the N-terminal D and E. Our analysis reveals multiple proteins with potential ATE1 target sites and expand our understanding of the biological complexity of the intracellular arginylome. |
| first_indexed | 2024-09-23T16:16:57Z |
| format | Article |
| id | mit-1721.1/129727 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T16:16:57Z |
| publishDate | 2021 |
| publisher | Springer Science and Business Media LLC |
| record_format | dspace |
| spelling | mit-1721.1/1297272022-10-02T07:33:49Z Target site specificity and in vivo complexity of the mammalian arginylome Wang, Junling Pejaver, Vikas Rao Dann, Geoffrey P. Wolf, Maxim Y. Kellis, Manolis Huang, Yun Garcia, Benjamin A. Radivojac, Predrag Kashina, Anna Massachusetts Institute of Technology. Computer Science and Artificial Intelligence Laboratory Protein arginylation mediated by arginyltransferase ATE1 is a key regulatory process essential for mammalian embryogenesis, cell migration, and protein regulation. Despite decades of studies, very little is known about the specificity of ATE1-mediated target site recognition. Here, we used in vitro assays and computational analysis to dissect target site specificity of mouse arginyltransferases and gain insights into the complexity of the mammalian arginylome. We found that the four ATE1 isoforms have different, only partially overlapping target site specificity that includes more variability in the target residues than previously believed. Based on all the available data, we generated an algorithm for identifying potential arginylation consensus motif and used this algorithm for global prediction of proteins arginylated in vivo on the N-terminal D and E. Our analysis reveals multiple proteins with potential ATE1 target sites and expand our understanding of the biological complexity of the intracellular arginylome. 2021-02-09T20:48:44Z 2021-02-09T20:48:44Z 2018-11 2018-06 2019-07-18T13:17:52Z Article http://purl.org/eprint/type/JournalArticle 2045-2322 https://hdl.handle.net/1721.1/129727 Wang, Junling et al. "Target site specificity and in vivo complexity of the mammalian arginylome." Scientific Reports 8, 1 (November 2018): 16177 © 2018 The Author(s) en http://dx.doi.org/10.1038/s41598-018-34639-6 Scientific Reports Creative Commons Attribution 4.0 International license https://creativecommons.org/licenses/by/4.0/ application/pdf Springer Science and Business Media LLC Nature |
| spellingShingle | Wang, Junling Pejaver, Vikas Rao Dann, Geoffrey P. Wolf, Maxim Y. Kellis, Manolis Huang, Yun Garcia, Benjamin A. Radivojac, Predrag Kashina, Anna Target site specificity and in vivo complexity of the mammalian arginylome |
| title | Target site specificity and in vivo complexity of the mammalian arginylome |
| title_full | Target site specificity and in vivo complexity of the mammalian arginylome |
| title_fullStr | Target site specificity and in vivo complexity of the mammalian arginylome |
| title_full_unstemmed | Target site specificity and in vivo complexity of the mammalian arginylome |
| title_short | Target site specificity and in vivo complexity of the mammalian arginylome |
| title_sort | target site specificity and in vivo complexity of the mammalian arginylome |
| url | https://hdl.handle.net/1721.1/129727 |
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