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A yeast polyamine acetyltransferase.

Bingsheng Liu¹, Ann Sutton, Rolf Sternglanz

¹Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5215, USA.

The Journal of Biological Chemistry

|February 23, 2005

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A newly identified yeast gene, PAA1, encodes a polyamine acetyltransferase. This enzyme

Area of Science:

Yeast genetics
Molecular biology
Biochemistry

Background:

Polyamines play crucial roles in cellular processes.
The function of polyamine acetylation in yeast was previously uncharacterized.

Purpose of the Study:

To identify and characterize a novel yeast gene involved in polyamine metabolism.
To elucidate the enzymatic activity and in vivo function of the PAA1 gene product.

Main Methods:

Gene cloning and recombinant protein expression.
Enzymatic assays for polyamine acetylation.
Analysis of yeast mutants (paa1) under various stress conditions.
Genetic interaction studies with SAGA complex and spt mutants.

Main Results:

Related Experiment Videos

The yeast gene PAA1 encodes a polyamine acetyltransferase (Paa1) that acetylates putrescine, spermidine, and spermine.
paa1 mutants exhibit sensitivity to hydroxyurea and synthetic temperature sensitivity with rad53-21.
Genetic interactions suggest Paa1 influences chromatin accessibility.
Overexpression of Paa1 leads to growth dependence on pantothenate or beta-alanine, confirming spermine as an in vivo target.

Conclusions:

PAA1 encodes a functional polyamine acetyltransferase in yeast.
Polyamines acetylated by Paa1 are involved in chromatin structure and accessibility.
Spermine, acetylated by Paa1, is essential for coenzyme A biosynthesis in yeast.