Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4

Article Abstract:

Sec4 and Ypt1 are Ras-related GTP-binding proteins encoded in Saccharomyces cerevisiae by the SEC4 and YPT1 genes, respectively. Ypt1 is involved in vesicular transport from the endoplasmic reticulum to the Golgi apparatus, while Sec4 is involved in the fusion of post-Golgi secretory vesicles with the plasma membrane. A previous study showed three structural domains in the GTP-binding proteins specify the stage at which Sec4 and Ypt1 act. Sec4/Ypt1 chimeric proteins were developed and were used to show that the three structural domains cooperate to specify Ypt1 function.

Biological transport, G proteins

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DSS4-1 is a dominant suppressor of sec4-8 that encodes a nucleotide exchange protein that aids Sec4p function

Article Abstract:

Genetic suppression analysis can be used to clone the gene dss4 which helps the protein Sec4p in the secretory pathway of yeast. Sec4p is a member of the ras superfamily which binds GTP, but knowledge of GDP action with ras proteins has been limited. The gene dss4 makes a 17K nucleotide exchange protein which acts as a stimulator of GDP dissociation. Thus, the gene is shown to be a dominant suppressor for sec4-8.

Suppression, Genetic, Suppressor mutation (Molecular genetics)

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A mammalian guanine-nucleotide-releasing protein enhances function of yeast secretory protein Sec4

Article Abstract:

A mammalian cDNA, mss4, has been isolated along with its protein Mss4 which helps the protein Sec4 in the secretory pathway of yeast. Sec4 is a member of the ras superfamily which binds GTP, but knowledge of GDP action with ras proteins has been limited. The protein Mss4 releases GDP and resembles the yeast protein Dss4. Mss4 also releases GDP from Ypt1 and Rab3a proteins but Mss4 does not release GDP from Ras2.

Antisense DNA

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