SUMOYlation | SUMO Protein | Post Translational Modifications

In molecular biology, SUMO (S mall U biquitin-like MO difier) proteins are a family of small proteins that are covalently attached to and detached from other proteins in cells to modify their function.

Small ubiquitin-related modifier (SUMO) is a member of the ubiquitin-like protein family and, like ubiquitin, SUMO can be covalently attached to lysine side chains in a variety of target proteins.

SUMO proteins are similar to ubiquitin in their folded structure but possess only about 20% homology to the amino acid sequence of ubiquitin. The number of SUMO genes varies among eukaryotes. SUMO proteins are conjugated to substrate proteins in a manner

本論文實驗藉由點突變方法製造出帶有SUMO化共有基序的SUMO-1 (D15V)、SUMO-1 (D15V/K17T) 及SUMO-1 (K25E) 三種SUMO-1突變株，以及失去SUMO化共有基序的SUMO-2突變株SUMO-2 (K11A)，並建立在in vitro或在大腸桿菌中進行的SUMO化系統，以及能表現帶有tag之SUMO的動物穩定細胞株，作為研究SUMO化作用的工具，並探討SUMO化共有基序對SUMO聚合作用造成的影響。

Posttranslational modification by small ubiquitin-like modifiers (SUMOs) is critical in regulating diverse cellular processes including gene expression, cell cycle progression, genome integrity, cellular metabolism, and inflammation and immunity.

Besides the characteristics of the traditional fusion tags above, SUMO protein has other advantages, such as small molecules, promoting folding and specific cleaved by SUMO protease 1.

A SUMO protein is a small ubiquitin-related modifier that can attach to target proteins, altering their activity, cellular location, or interactions with other proteins through a series of enzymatic reactions involving E1, E2, and E3 enzymes.