Effect of cAMP-dependent Phosphodiesterase Activity on NTH1 Gene Expression and Reserve Carbohydrate Metabolism

Tulay Turgut Genc

Article Details

Effect of cAMP-dependent Phosphodiesterase Activity on NTH1 Gene Expression and Reserve Carbohydrate Metabolism

Authors:

Tulay Turgut Genc

Publisher:

Bingol University

Main Topics:

Sinyal İletimi | Biyokimya ve Hücre Biyolojisi (Diğer)

Journal:

Türk Doğa ve Fen Dergisi Vol.13 Issue 2, pp.106-113

Document Type:

Article

Publication Date:

6/2024

Document Language:

English

Document ID (Org No.):

2001321144

pISSN:

2149-6366

Keywords:

Abstract:

 Protein kinase A signaling pathway is regulated by cAMP. PKA activity is inhibited by the cAMP phosphodiesterases. PDE1 and PDE2 genes encode two phosphodiesterases with low and high affinity for cAMP, respectively. NTH1 gene encodes the neutral trehalase enzyme, which is responsible for the stress-accumulated trehalose degradation. This study aimed to investigate the effect of PDE1 and PDE2 gene products on the expression of the NTH1 gene and reserve carbohydrate metabolism in response to a stressful environment and during a replenishment phase. The expression of the NTH1 gene was shown to be lower than that of the wild-type under normal conditions, heat stress, nitrogen starvation, and also during the replenishment period in pde1 and pde1 yeast cells. The accumulation of trehalose and glycogen was shown to be dramatically enhanced in pde1 yeast cells. However, deletion of the PDE2 gene did not lead to a significant change in trehalose and glycogen accumulation comparable to that found in the wild type. These results indicate that the PDE1 gene product is required for downregulation of reserve carbohydrate metabolism. Consequently, the Pde1 protein is considered to exert yet-unidentified regulatory control over the Pde2 protein.

 Protein kinase A signaling pathway is regulated by cAMP. PKA activity is inhibited by the cAMP phosphodiesterases. PDE1 and PDE2 genes encode two phosphodiesterases with low and high affinity for cAMP, respectively. NTH1 gene encodes the neutral trehalase enzyme, which is responsible for the stress-accumulated trehalose degradation. This study aimed to investigate the effect of PDE1 and PDE2 gene products on the expression of the NTH1 gene and reserve carbohydrate metabolism in response to a stressful environment and during a replenishment phase. The expression of the NTH1 gene was shown to be lower than that of the wild-type under normal conditions, heat stress, nitrogen starvation, and also during the replenishment period in pde1 and pde1 yeast cells. The accumulation of trehalose and glycogen was shown to be dramatically enhanced in pde1 yeast cells. However, deletion of the PDE2 gene did not lead to a significant change in trehalose and glycogen accumulation comparable to that found in the wild type. These results indicate that the PDE1 gene product is required for downregulation of reserve carbohydrate metabolism. Consequently, the Pde1 protein is considered to exert yet-unidentified regulatory control over the Pde2 protein.

 Protein kinase A signaling pathway is regulated by cAMP. PKA activity is inhibited by the cAMP phosphodiesterases. PDE1 and PDE2 genes encode two phosphodiesterases with low and high affinity for cAMP, respectively. NTH1 gene encodes the neutral trehalase enzyme, which is responsible for the stress-accumulated trehalose degradation. This study aimed to investigate the effect of PDE1 and PDE2 gene products on the expression of the NTH1 gene and reserve carbohydrate metabolism in response to a stressful environment and during a replenishment phase. The expression of the NTH1 gene was shown to be lower than that of the wild-type under normal conditions, heat stress, nitrogen starvation, and also during the replenishment period in pde1 and pde1 yeast cells. The accumulation of trehalose and glycogen was shown to be dramatically enhanced in pde1 yeast cells. However, deletion of the PDE2 gene did not lead to a significant change in trehalose and glycogen accumulation comparable to that found in the wild type. These results indicate that the PDE1 gene product is required for downregulation of reserve carbohydrate metabolism. Consequently, the Pde1 protein is considered to exert yet-unidentified regulatory control over the Pde2 protein.

 Protein kinaz A sinyal yolağı cAMP tarafından düzenlenir. PKA aktivitesi, cAMPyi hidrolize eden cAMP fosfodiesterazlar tarafından inhibe edilir. PDE1 ve PDE2 genleri cAMP için düşük ve yüksek afiniteye sahip iki fosfodiesterazı kodlar. NTH1 geni stres şartlarında biriktirilen trehalozun parçalanmasından sorumlu olan nötral trehalaz enzimini kodlar. Bu çalışmada, stres koşullarında ve stres sonrasında, PDE1 ve PDE2 genlerinin NTH1 gen ekspresyonu ve depo karbonhidrat metabolizması üzerine etkisinin belirlenmesi amaçladı. Normal koşullarda, ısı stresinde, azot açlığında ve stresten kurtulma sonrasında, pde1 ve pde1 maya hücrelerinde belirlenen NTH1 gen ekspresyonunun yaban tipten daha düşük olduğu görüldü. Trehaloz ve glikojen birikiminin pde1 maya hücrelerinde oldukça yüksek oranda arttığı gözlendi. Bununla birlikte, PDE2 yokluğunun trehaloz ve glikojen birikiminde önemli bir değişikliğe yol açmadığı gözlendi. Bu sonuçlar, depo karbonhidrat metabolizmasının aşağı regülasyonu için PDE1 gen ürününün gerekli olduğunu göstermektedir. Sonuç olarak, Pde1 proteininin, Pde2 proteini üzerinde henüz tanımlanamayan düzenleyici kontrol uyguladığı düşünülmektedir.

Article Details

Effect of cAMP-dependent Phosphodiesterase Activity on NTH1 Gene Expression and Reserve Carbohydrate Metabolism

Authors:

Tulay Turgut Genc

Publisher:

Bingol University

Main Topics:

Sinyal İletimi | Biyokimya ve Hücre Biyolojisi (Diğer)

Journal:

Türk Doğa ve Fen Dergisi Vol.13 Issue 2, pp.106-113

Document Type:

Article

Publication Date:

6/2024

Document Language:

English

Document ID (Org No.):

2001321144

pISSN:

2149-6366

Heat stress

Nitrogen starvation

PDE1

PDE2

Saccharomyces cerevisiae

Stress recoveryIsı stresi

Azot açlığı

PDE1

PDE2

Saccharomyces cerevisiae

Stresten kurtulma

Issues

Article Details

Authors: Tulay Turgut Genc

Publisher: Bingol University

Main Topics: Sinyal İletimi | Biyokimya ve Hücre Biyolojisi (Diğer)

Journal: Türk Doğa ve Fen Dergisi Vol.13 Issue 2, pp.106-113

Document Type: Article

Publication Date: 6/2024

Document Language: English

Document ID (Org No.): 2001321144

pISSN: 2149-6366

Issues

Authors:

Tulay Turgut Genc

Publisher:

Bingol University

Main Topics:

Sinyal İletimi | Biyokimya ve Hücre Biyolojisi (Diğer)

Journal:

Türk Doğa ve Fen Dergisi Vol.13 Issue 2, pp.106-113

Document Type:

Article

Publication Date:

6/2024

Document Language:

English

Document ID (Org No.):

2001321144

pISSN:

2149-6366