Disease relevance of RPP2A

• Cell cycle function of a Medicago sativa A2-type cyclin interacting with a PSTAIRE-type cyclin-dependent kinase and a retinoblastoma protein [1].

High impact information on RPP2A

• By gene disruption techniques with linearized DNA from these constructions, strains of Saccharomyces cerevisiae were obtained which lacked a functional gene for either protein L44 or protein L45 [2].
• These data suggest that TOG mediates the association of hnRNP A2-positive granules with microtubules during transport and/or localization [3].
• In neural cells, such as oligodendrocytes and neurons, transport of certain RNAs along microtubules is mediated by the cis-acting heterogeneous nuclear ribonucleoprotein A2 response element (A2RE) trafficking element and the cognate trans-acting heterogeneous nuclear ribonucleoprotein (hnRNP) A2 trafficking factor [3].
• TOG coimmunoprecipitates with hnRNP A2 present in the cytoskeleton (CSK) fraction of neural cells, and both coprecipitate with microtubule stabilized pellets [3].
• Sequencing of tryptic phosphopeptides has shown that acidic proteins YP1 alpha and YP2 alpha (L44) are also phosphorylated at positions near the carboxyl end [4].

Biological context of RPP2A

• These results indicated that proteins L44 and L45 are independently dispensable for cell growth and that the ribosome is functional in the absence of either of them [2].
• By using site-directed mutagenesis and chemical analysis of phosphopeptides, a unique phosphorylation site has been shown at serine 73 in the amino acid sequence of the Saccharomyces cerevisiae acidic ribosomal protein YP1 beta (L44') [4].
• DNA probes from the genes encoding the acidic ribosomal proteins L44, L44' and L45, as well as from reporter genes for chromosomes IV, VII, XII and XV, have been hybridised to Southern blots of Saccharomyces cerevisiae DNA resolved by pulsed field gel electrophoresis [5].
• Like most ribosomal protein genes, the gene for protein L44' has an intron and two upstream stimulatory boxes (UASrpg) fitting closely to the consensus sequence [6].
• The genes coding for proteins L44 and L45 lack introns and seem also exceptional in other characteristics of their sequences [6].

Anatomical context of RPP2A

• The RPL44' gene from Saccharomyces cerevisiae encoding the ribosomal protein YP1 beta(L44') has been found to be linked to the STF1 gene, encoding a stabilizing factor of the F1F0-ATPase inhibitor protein from mitochondria [7].

Associations of RPP2A with chemical compounds

• Two-dimensional polyacrylamide-gel electrophoretic analysis of yeast ribosomal proteins labelled in vivo with 32PO43- revealed that the proteins S2 and S10 of the 40S ribosomal subunit, and the proteins L9, L30, L44 and L45 of the 60S ribosomal subunit, are phosphorylated in vivo [8].
• Core particles derived from yeast ribosomes by treatment with 50% ethanol and 0.4 M NH4Cl (P0.4 cores) are derived of the acidic proteins L44/45 functionally equivalent to the bacterial proteins L7 and L12 [9].
• Furthermore, the secretion of alpha-amylase activity is drastically repressed by glucose in both Sw. occidentalis and a transformant of S. cerevisiae containing SW A2 [10].
• Wild-type and mutant receptors were expressed in yeast cells and assayed for their ability to transactivate an estrogen-responsive reporter plasmid (ERE-CYCl-LacZ) that contained a single estrogen response element of the vitellogenin A2 gene promoter [11].
• Upon genetically deleting the glycosylation site, the level of secretion decreased to 3.6 mg prophospholipase A2 per 1 [12].

Physical interactions of RPP2A

• We previously identified an alternatively spliced variant of the chicken A subunit in which a 30 amino acid cassette (A1) containing the Walker consensus sequence for ATP binding is replaced by a 24 amino acid cassette (A2) that lacks this feature [13].

Other interactions of RPP2A

• Purified ribosomal proteins together with specific rabbit antisera were used to identify the two smaller rRNP antigens as the acidic phosphoproteins of the large ribosomal subunit, designated P1/P2(L40/L41) (rat), eL7/eL12 (Artemia, brine shrimp), and A1/A2 (yeast) [14].

Analytical, diagnostic and therapeutic context of RPP2A

• The use of genetic engineering to obtain efficient production of porcine pancreatic phospholipase A2 by Saccharomyces cerevisiae [12].

References