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Post-translational modifications of chicken myelin basic protein charge components
Jeongkwon Kim1, Rui Zhang, Eric F Strittmatter
1Environmental Molecular Sciences Laboratory, MSIN K8-98, Pacific Northwest National Laboratory, P.O. Box 999, Richland, WA 99352, USA.
Neurochemical Research
|July 12, 2008
Summary
Chicken myelin basic protein (MBP) exhibits unique post-translational modifications (PTMs) compared to mammals. Researchers identified distinct phosphorylation and deamidation patterns in chicken MBP charge components C1-C3.
Area of Science:
- Neuroscience
- Biochemistry
- Proteomics
Background:
- Myelin basic protein (MBP) is a key component of the myelin sheath in the central nervous system.
- MBP exists in various post-translationally modified forms (charge components/isomers) across different species.
- Chicken MBP displays a different charge component profile compared to mammalian MBP.
Purpose of the Study:
- To characterize the post-translational modifications (PTMs) of chicken MBP charge components C1, C2, and C3.
- To compare the PTMs of chicken MBP with those found in other vertebrate species.
Main Methods:
- Purification of chicken MBP and isolation of charge components C1, C2, and C3.
- Enzymatic digestion of isolated components using trypsin and endoproteinase Glu-C.
- Analysis of digests using capillary liquid chromatography coupled with tandem mass spectrometry (ion trap and FT-ICR).
Main Results:
- N-terminal acetylation was observed in all analyzed chicken MBP components.
- Component C1 lacked phosphorylation but contained R105 methylation; C2 and C3 also had R105 methylation.
- Component C2 had ten phosphorylation sites and citrulline at R24 and R165; C3 had eight phosphorylation sites and citrulline at R41, R24, and R165.
- Partial deamidation of glutamine (Q71, Q101, Q146) and asparagine (N90) was detected across components.
- Chicken MBP shares some phosphorylated serine and threonine residues with mammalian MBP but differs significantly from dogfish MBP.
Conclusions:
- Chicken MBP charge components C1-C3 possess distinct and partial post-translational modifications, including phosphorylation, methylation, deamidation, and citrullination.
- The PTM profile of chicken MBP differs notably from mammalian and fish MBP, particularly in phosphorylation patterns.
- These species-specific PTMs may contribute to functional variations in MBP across vertebrates.
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