Part:BBa_K4609056
HSP 27-6xHis
A heat shock protein. During the synthesis of Hsp27, Escherichia coli consumes glucose, the glucose metabolic pathway is regulated, and the lactose pathway is activated, increasing the lactose concentration in Escherichia coli, thereby leading to protein expression. Or Hsp27 interacts with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in E. coli. GAPDH is encoded by Escherichia coli gapA gene, and the affinity between Hsp27 and GAPDH is strong. GAPDH is the sixth enzyme in the glycolytic pathway. Disturbance of this enzyme can directly alter glycolysis, thus altering the entire bacterial metabolism, transforming the glycolytic pathway into the lactose pathway, increasing lactose concentration in E. coli, and ultimately leading to protein expression.
In addition, Hsp27 has a protective effect on cornea in the eye. Phosphorylated Hsp27 is highly expressed in corneal surface epithelial cells during corneal epithelial wound healing, and phosphorylation of Hsp27 plays a role in cell component reconstruction and cell migration. This phosphorylated protein has anti-apoptotic properties, and its surface localization confers innate corneal defense and corneal barrier functions.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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