Chemical and Functional Aspects of Posttranslational Modification of Proteins

Abstract

this paper reviews the chemical and functional aspects of the posttranslational modifications of proteins, which are achieved by the addition of various groups to the side chain of the amino acid residue backbone of proteins. It describes the main prosthetic groups and the interaction of these groups and the apoenzyme in the process of catalysis, using pyridoxal catalysis as an example. Much attention is paid to the role of posttranslational modification of proteins in the regulation of biochemical processes in live organisms, and especially to the role of protein kinases and their respective phosphotases. Methylation and acetylation reactions and their role in the "histone code," which regulates genome expression on the transcription level, are also reviewed. this paper also describes the modification of proteins by large hydrophobic residues and their role in the function of membrane-associated proteins. Much attention is paid to the glycosylation of proteins, which leads to the formation of glycoproteins. We also describe the main non-enzymatic protein modifications such as glycation, homocysteination, and desamidation of amide residues in dibasic acids. Abbreviations: coA -coenzyme A, eGFr -epidermal growth factor receptor, JnK -Jun N-terminal kinase, SAPK -stress activated protein kinase, МАРК -mutagen-activated protein kinase, IF -inositoltriphosphate, DAG -diacylglycerol, JAK -Janus kinase, StAt -signal transducer and activator of transcription, Fyn, Lck -non-receptor tyrosinekinases of the Src family, ub -ubiquitin residue, uLP -ubiquitin-like protein, ras, rab, rho -protein products of the protooncogenes ras, rab, rho, which play a role in cell growth and differentiation, SАМ -S-adenosylmethinone, PArP -poly(ADP-ribose)polymerase, VrAP -telomerase, found to be a part of vault particles, GSH -glutathione, HIF -hypoxia inducible factor, Gla -γ-carboxyglutamic acid, AGe -advanced glycation end products, cML -N ε -carboxymethyl-lysine, ceL -N ε -carboxyethyl-lysine, HSA -human serum albumin, GFP -green fluorescent protein, РIMt -protein isoaspartyl-О-methyltransferase, Dnt -dermonecrotic toxin.

The phosphorylation of the N protein could affect PRRSV virulence in vivo

“…PTMs occurs during or after protein biosynthesis (Knorre et al, 2009). It plays an important role in many biological processes, such as protein degradation, regulation of gene expression and protein function state.…”

“…Post-translation modifications (PTM) occur during or after protein biosynthesis (Knorre et al, 2009). Including phosphorylation, acetylation, glycosylation, SUMOylation, many proteins contain PTM, and the protein functions can be regulated by those modifications (Xu et al, 2018a;Yang et al, 2019).…”

Producción de proteínas recombinantes a partir de animales transgénicos: Sistemas y aplicaciones

“…Se trata de una modificación, ya sea en los grupos hidroxilo de los residuos de serina y de treonina (O-glicosilación) o en los grupos funcionales de las cadenas laterales de los residuos de asparagina (N-glicosilación). Otras modificaciones importantes de este tipo en mamíferos son la carboxilación de factores de coagulación en los residuos de ácido γ-carboxiglutámico, la adición de un residuo de sulfato en el grupo OH de la tirosina y la adición de grupos fosfato a cadenas laterales de aminoácidos (fosforilación) [21].…”

T54R mutation destabilizes the dimer of superoxide dismutase 1T54R by inducing steric clashes at the dimer interface

“…3 The order of a protein's folding and dynamic stability also depends upon complex cellular machineries like chaperones and posttranslational modiers. 4,5 The events of regulated and stoichiometrically dened oligomerization of proteins are required for their optimal stability and functionality. 6 In a stable oligomer, critical residues at the interface of subunits mediate necessary interactions with the residues of other subunits.…”