Phosphorylation of basic amino acid residues in proteins: important but easily missed.

Abstract

Reversible phosphorylation is the most widespread posttranslational protein modification, playing regulatory role in almost every aspect of cell life. The majority of protein phosphorylation research has been focused on serine, threonine and tyrosine that form acid-stable phosphomonoesters. However, protein histidine, arginine and lysine residues also may undergo phosphorylation to yield acid-labile phosphoramidates, most often remaining undetected in conventional studies of protein phosphorylation. It has become increasingly evident that acid-labile protein phosphorylations play important roles in signal transduction and other regulatory processes. Beside acting as high-energy intermediates in the transfer of the phosphoryl group from donor to acceptor molecules, phosphohistidines have been found so far in histone H4, heterotrimeric G proteins, ion channel KCa3.1, annexin 1, P-selectin and myelin basic protein, as well as in recombinant thymidylate synthase expressed in bacterial cells. Phosphoarginines occur in histone H3, myelin basic protein and capsidic protein VP12 of granulosis virus, whereas phospholysine in histone H1. This overview of the current knowledge on phosphorylation of protein basic amino-acid residues takes into consideration its proved or possible roles in cell functioning. Specific requirements of studies on acid-labile protein phosphorylation are also indicated.

Intrinsic size parameters for palmitoylated and carboxyamidomethylated peptides

“…56–7 And for phosphorylation studies, the phosphate group can be on Ser, Thr, Tyr, His, Arg and Lys. 47 To probe all of the combinations would be tedious and demanding, yet to obtain enough data for a mixture of the combinations would be much more reasonable.…”

Unification of [FeFe]-hydrogenases into three structural and functional groups

“…Protein kinases have been a subject of extensive study which have demonstrated their involvement in various regulatory processes. Among those most widely studied are Hkl and Stk which have been biochemically shown to target histidine (H) and serine/threonine (S/T) for phosphorylation, respectively [70,[80][81][82][83]. The presence of Hkl and Stk in the gene neighborhood of G3 hydA indicate that these kinases and phosphatases may be involved in reversible phosphorylation of H, S and T residues.…”

Post‐translational modification: nature's escape from genetic imprisonment and the basis for dynamic information encoding

“… Notes: 1 Reversible phosphorylation on histidine and aspartate forms the basis for two-component signalling, which is abundant in eubacteria and is also found in plants and fungi (100); acidlabile phosphoramidate attachments to basic residues are also found in eukaryotes (18). …”