(mở đầu)

● Hello everyone, My name is Huy. Next, we're diving into nitrogen

metabolism regulation by post-translational modifications of PII proteins.

● PII proteins are a widespread family participating in the signal transduction

pathway found in Bacteria, Archaea (a kia a), and the plastids of plants.

● PII proteins are crucial for the metabolism of nitrogen.

● In this example, PII activity is regulated by uridylylation mediated by GlnD, a

bifunctional enzyme that possesses both uridylyltransferase (đọc là diu ri đi lin trans
phơ ray) activity and uridyl-removal activity in accordance with the levels of the
glutamine.

(trường hợp không có glutamine)

● When the cellular concentration (cần xơ tray sần) of glutamine is low, NH3
assimilation is required and GlnD not bound to glutamine will add a UMP
group to PII.

The PII-UMP (đọc là bi tai tu u em bi) increases by post-translational

modification triggers removal of adenyl groups from glutamine synthetase
(GS).

As more adenyl groups are removed from GS, its activity increases and NH3
assimilation also increases

(trường hợp có glutamine)

● The binding of glutamine to GlnD inhibits uridylylation.

PII proteins are deactivated.

● PII proteins activate glutamine synthetase adenyltransferase (đọc là a đê nin

trans phơ ray)

GS activity is decreased and NH3 assmilation is reduced

(giải thích sự cần thiết của cơ chế)

This regulation of PII is necessary because GS is energy-consuming and must be
tightly regulated to conserve energy

GS can assimilate amonia even at very low concentrations (cần xơ tray sần), but cost a
lot of energy.

Actually, NH3 can be converted into amino acids by enzymes that do not need ATP

By increasing the activity of GS only when NH3 is limiting, the cell can conserve the
ATP needed for other energy-consuming processes.

● Thank you for your attention. Please feel free to raise questions if you have
any.