Posttranslational Protein Modification by Amino Acid Addition in Regenerating Optic Nerves of Goldfish

1986 ◽  
Vol 46 (3) ◽  
pp. 726-732 ◽  
Author(s):  
G. Chakraborty ◽  
T. Leach ◽  
M. F. Zanakis ◽  
N. A. Ingoglia
Keyword(s):  
Amino Acid ◽  
Protein Modification ◽  
Optic Nerves ◽  
Acid Addition ◽  
Posttranslational Protein Modification

Protein modification by amino acid addition is increased in crushed sciatic but not optic nerves

Science ◽  
1986 ◽  
Vol 231 (4738) ◽  
pp. 603-605 ◽  
Author(s):  
S Shyne-Athwal ◽  
R. Riccio ◽  
G Chakraborty ◽  
N. Ingoglia
Keyword(s):  
Amino Acid ◽  
Protein Modification ◽  
Optic Nerves ◽  
Acid Addition

scholarly journals The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Erna Davydova ◽  
Tadahiro Shimazu ◽  
Maren Kirstin Schuhmacher ◽  
Magnus E. Jakobsson ◽  
Hanneke L. D. M. Willemen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Function ◽  
Crucial Role ◽  
Complex I ◽  
Protein Modification ◽  
Zinc Binding ◽  
Functional Studies ◽  
Mitochondrial Respiratory Complex ◽  
Respiratory Complex I ◽  
Broad Specificity

AbstractPost-translational methylation plays a crucial role in regulating and optimizing protein function. Protein histidine methylation, occurring as the two isomers 1- and 3-methylhistidine (1MH and 3MH), was first reported five decades ago, but remains largely unexplored. Here we report that METTL9 is a broad-specificity methyltransferase that mediates the formation of the majority of 1MH present in mouse and human proteomes. METTL9-catalyzed methylation requires a His-x-His (HxH) motif, where “x” is preferably a small amino acid, allowing METTL9 to methylate a number of HxH-containing proteins, including the immunomodulatory protein S100A9 and the NDUFB3 subunit of mitochondrial respiratory Complex I. Notably, METTL9-mediated methylation enhances respiration via Complex I, and the presence of 1MH in an HxH-containing peptide reduced its zinc binding affinity. Our results establish METTL9-mediated 1MH as a pervasive protein modification, thus setting the stage for further functional studies on protein histidine methylation.

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