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The lysine residue of proteins may undergo many types of chemical modification including acetylation, phosphorylation,ubiquitination, lipidation and methylation. In acetylation, the lysine group may serve as a donor or acceptor of acetyl moieties.
Lysine modifications affect the secondary, tertiary and quaternary structures of proteins as well as their cellular functions. In

1/2some cases, post-translational modifications allow protein isoforms, alternate splice variants, or transient intermediates to befunctionally and structurally distinct from their mature protein counterparts. Recently, it has become possible to assay some ofthe post-translational modification processes in vitro and in vivo. These include lysine acetylation and deacetylation, proteolytic
processing of proteins, and lysine methylation, acetylation, and ubiquitination. This article examines these processes from abiochemical perspective, with an emphasis on the role of proteins in cell regulation and differentiation.Regulation of IL-2
production and memory induction by suppressive CD4+CD25+ T cells. We previously reported that asplenic mice wereresistant to lipopolysaccharide (LPS) injection because of impaired IL-2 production. The CD4(+)CD25(+) T cells (T(reg)) inthe spleen, lymph node and bone marrow (BM) of asplenic mice express Foxp3, and are generated and activated at normal levels
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