A novel Chlamydomonas reinhardtii gene potentially encoding a proline-, glycine-, and tyrosine-rich protein (PGYRP)

Isolation and characterization of both the cDNA and the gene coding for a novel Chlamydomonas reinhardtii protein are here reported. Some peculiar features reported for Chlamydomonas species are recognizable in this mRNA, whose expression resulted to be heat-sensitive. The corresponding nuclear gene...

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Bibliographic Details
Published in:Plant science (Limerick) 2004-09, Vol.167 (3), p.519-526
Main Authors: Sangiorgio, Lorenzo, Strumbo, Bice, Tenchini, Maria L., Malcovati, Massimo, Ronchi, Severino, Simonic, Tatjana
Format: Article
Language:English
Subjects:
algae and seaweeds
amino acid sequences
Biological and medical sciences
cDNA
Chlamydomonas reinhardtii
complementary DNA
Fundamental and applied biological sciences. Psychology
Gene
gene expression regulation
Genes. Genome
Heat shock-responsive elements
heat stress
messenger RNA
Molecular and cellular biology
Molecular genetics
molecular sequence data
nucleotide sequences
plant proteins
proline-, glycine-, and tyrosine-rich protein
Proline-, glycine-, and tyrosine-rich protein (PGYRP)
promoter regions
sequence analysis
TATA box
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Summary:Isolation and characterization of both the cDNA and the gene coding for a novel Chlamydomonas reinhardtii protein are here reported. Some peculiar features reported for Chlamydomonas species are recognizable in this mRNA, whose expression resulted to be heat-sensitive. The corresponding nuclear gene exhibits nine introns, all interrupting the coding region and is preceded by a proximal promoter region showing a putative TATA box and a number of sequences fitting heat shock-responsive elements. The deduced protein comprises 169 amino acids and has been called proline-, glycine-, and tyrosine-rich protein (PGYRP), due to the high content of these residues (about 30, 20, and 15%, respectively). The N-terminal region is proline-rich and contains several tandemly repeated hexapeptides sharing the consensus P[Q/P][P/A]GYP, the C-terminal region is rich in glycine, histidine, and lysine, therefore extremely basic; both these domains could be able to interact with other proteins. PGYRP may play a role as adaptor, involved in one or several cellular functions.
ISSN:0168-9452
1873-2259
DOI:10.1016/j.plantsci.2004.04.019