High impact information on ATPRP1

• Although the NLY protein shares extensive sequence similarity with its angiosperm counterparts, it is lacking the proline-rich and acidic motifs thought to function as transcriptional activation domains [1].
• Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides [2].
• The recombinant P4H effectively hydroxylated poly(l-proline) and many synthetic peptides corresponding to proline-rich repeats present in plant glycoproteins and other proteins [2].
• However, efficient suppression of yeast PCD occurred by expression of a chimeric gene, composed of the conserved domains from yeast, fused to the variable N-terminal domain from Arabidopsis, resulting in exchange of the proline-rich N-terminal domain of SCN2 with a proline-poor Arabidopsis sequence [3].
• Our results suggest that intracellular vesicle traffic can regulate execution of apoptosis by affecting the rate of membrane recycling and that the proline-rich N-terminal domain of VAMP inhibited this process [3].

Biological context of ATPRP1

• The AtEPR1 open reading frame consists of 40 proline-rich repeats and is expressed in both wild-type and mutant lines [4].
• The primary protein structures predicted from the cDNA sequences revealed that the regions around both the heme-binding site and the proline-rich motif were highly conserved among all these P450s [5].
• A novel zinc-finger protein with a proline-rich domain mediates ABA-regulated seed dormancy in Arabidopsis [6].
• We report the isolation and characterization of PERKI (Proline Extensin-like Receptor Kinase 1), a novel plant RLK from Brassica napus that is predicted to consist of a proline-rich extracellular domain with sequence similarity to extensins, a transmembrane region, and a catalytic domain possessing serine/threonine kinase activity [7].

Anatomical context of ATPRP1

• Characterization and expression of four proline-rich cell wall protein genes in Arabidopsis encoding two distinct subsets of multiple domain proteins [8].
• The retention of gamma-zein in the endoplasmic reticulum was found to be mediated by structural features contained in the polypeptide, an N-terminal proline-rich and a C-terminal cysteine-rich domain which were necessary for the correct retention and assembly of gamma-zein within protein bodies (M.I. Geli et al., 1994, Plant Cell 6: 1911-1922) [9].

Associations of ATPRP1 with chemical compounds

• Sequence analysis revealed that AIR1 encodes a protein that is related to a large family of proteins that consist of a proline-rich or glycine-rich N-terminus and a hydrophobic, possibly membrane spanning C-terminus [10].
• In the present work we incorporated in the gamma-zein gene lysine-rich coding sequences which were positioned after the N-terminal proline-rich domain and at five amino-acid residues from the C-terminus [9].
• These results suggest that this novel zinc-finger protein with a proline-rich N-terminus is an important downstream component of the ABA signaling pathway that mediates ABA-regulated seed dormancy in Arabidopsis [6].
• Their carboxyl-terminal halves, although less similar to each other, included glutamine-rich and proline-rich regions characteristic of the transcriptional activation domain of eukaryotes [11].

Other interactions of ATPRP1

• Expression of AtPRP3, a proline-rich structural cell wall protein from Arabidopsis, is regulated by cell-type-specific developmental pathways involved in root hair formation [12].
• The Arabidopsis thaliana PROTODERMAL FACTOR1 (PDF1) gene encoding a putative extracellular proline-rich protein is exclusively expressed in the L1 layer of shoot apices and the protoderm of organ primordia [13].
• Genomic and cDNA clones of the anther-specific APG gene from Arabidopsis thaliana and Brassica napus, which encodes a novel proline-rich protein, were isolated and characterized [14].
• The proline-rich, extensin-like receptor kinase-1 (PERK1) gene is rapidly induced by wounding [7].

References