Mapping the Phosphorylation Pattern of Drosophila melanogaster RNA Polymerase II Carboxyl-Terminal Domain Using Ultraviolet Photodissociation Mass Spectrometry
| Autor: | Jennifer S. Brodbelt, Joe R. Cannon, Anjana Ram, Yan Jessie Zhang, David S. Gilmour, Seema Irani, Victoria C. Cotham, Wendy L. Matthews, Joshua E. Mayfield, Michelle R. Robinson |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Ultraviolet Rays Protein domain RNA polymerase II Saccharomyces cerevisiae Computational biology environment and public health Biochemistry Article Mass Spectrometry 03 medical and health sciences Protein Domains Animals Amino Acid Sequence Phosphorylation Peptide sequence Polymerase Mitogen-Activated Protein Kinase 1 Genetics biology fungi Eukaryotic transcription General Medicine biology.organism_classification enzymes and coenzymes (carbohydrates) Drosophila melanogaster 030104 developmental biology biology.protein Molecular Medicine RNA Polymerase II CTD Protein Processing Post-Translational |
| Zdroj: | ACS Chemical Biology. 12:153-162 |
| ISSN: | 1554-8937 1554-8929 |
| DOI: | 10.1021/acschembio.6b00729 |
| Popis: | Phosphorylation of the C-terminal domain of RNA polymerase II (CTD) plays an essential role in eukaryotic transcription by recruiting transcriptional regulatory factors to the active polymerase. However, the scarcity of basic residues and repetitive nature of the CTD sequence impose a huge challenge for site-specific characterization of phosphorylation, hindering our understanding of this crucial biological process. Herein, we apply LC-UVPD-MS methods to analyze post-translational modification along native sequence CTDs. Application of our method to the Drosophila melanogaster CTD reveals the phosphorylation pattern of this model organism for the first time. The divergent nature of fly CTD allows us to derive rules defining how flanking residues affect phosphorylation choice by CTD kinases. Our data support the use of LC-UVPD-MS to decipher the CTD code and determine rules that program its function. |
| Databáze: | OpenAIRE |
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