Disease relevance of RPLP1

• Anti-P antibodies present in sera from patients with chronic Chagas heart disease (cChHD) recognize peptide R13, EEEDDDMGFGLFD, which encompasses the C-terminal region of the Trypanosoma cruzi ribosomal P1 and P2 proteins [1].
• Two forms of gonadotropin-releasing hormone (GnRH) are expressed in human breast tissue and overexpressed in breast cancer: a putative mechanism for the antiproliferative effect of GnRH by down-regulation of acidic ribosomal phosphoproteins P1 and P2 [2].
• The ability of the chimeric RNA to replicate in the absence of capsid formation was measured after replacement of the P1 region with a luciferase reporter gene [3].
• 2A protease (2Apro) catalyzes the initial cleavage of the poliovirus polyprotein which separates the P1 structural protein precursor from the P2-P3 nonstructural protein precursor [4].
• The outer membrane proteins (OMPs) P1 and P2 of Haemophilus influenzae type b exhibit molecular size and antigenic variation [5].

High impact information on RPLP1

• METHODS: In situ RNA hybridization was used with two human liver samples and specific probes for the phenol transferase RNA, HLUG P1, and the bilirubin transferase RNAs, HUG-Br1 and HUG-Br2 [6].
• Moreover moving the native ctrA gene to a position near the chromosomal terminus, which delays the conversion of the ctrA promoter from the fully to the hemimethylated state until late in the cell cycle, inhibited ctrA P1 transcription, and altered the time of accumulation of the CtrA protein and the size distribution of swarmer cells [7].
• Passage 1 (P1) and P10 cells have identical morphology, immunophenotype, telomere length, and differentiation capacity [8].
• Whole-cell patch-clamp recordings of S49 lymphoma cells show a P1-dependent inward membrane current flow in the presence but not in the absence of Ca2+ [9].
• P1 site-specific recombination: nucleotide sequence of the recombining sites [10].

Chemical compound and disease context of RPLP1

• Neither the absence nor the overproduction of P1 affected expression of capsular polysaccharide and lipooligosaccharide by Hib [11].
• Identification of a new P1 residue mutation (444Arg----Ser) in a dysfunctional C1 inhibitor protein contained in a type II hereditary angioedema plasma [12].
• Polymorphism in the glutathione S-transferase P1 gene and risk for preeclampsia [13].

Biological context of RPLP1

• The identities of the P1 and P2 cDNAs were confirmed by the strong similarities of their encoded amino acid sequences to published primary structures of the homologous rat, brine shrimp, and Saccharomyces cerevisiae proteins [14].
• By a yeast two-hybrid system, ribosomal phosphoproteins P0 and P1 and a putative mitotic checkpoint protein, MAD2B, were found to interact with an active-site mutated trichosanthin (TCS) [15].
• The P1 and P2 proteins interact with elongation factors EF1 and EF2, and the level of their phosphorylation is one of the regulatory mechanisms for the overall rate of protein elongation [2].
• Accordingly we propose that this gene cluster may have arisen from the P1 gene through a series of gene duplication events [16].
• This new genomic organisation revealed that all known chromosomal translocations map upstream of P2, removing P1 and putative upstream regulatory sequences leaving P2 intact [17].

Anatomical context of RPLP1

• The synthetic P0, P1, and P2 proteins were serologically and electrophoretically identical to P-proteins extracted from HeLa cells [14].
• In eukaryotes, this ribosomal structure is composed of the acidic ribosomal P proteins, forming two hetero-dimers (P1/P2) attached to the ribosome through the P0 protein [18].
• METHODS: Anti-P mAbs were prepared by a standard hybridoma procedure using recombinant human P1 and P2 proteins as immunogens [19].
• Patients with abnormal P1/P2 ratios displayed significantly reduced semen quality and sperm penetration ability [20].
• Two basic proteins, denoted P1 and P2 protein, were purified from human sciatic nerve [21].

Associations of RPLP1 with chemical compounds

• In order to map the immunodominant domains of the E1 glycoprotein, two epitopes from amino acid residues 210 to 223 (P1) and 315 to 327 (P2) were predicted from the HCV sequence [22].
• P1 enzyme was already purified and identified as a subtilisin-like serine endoprotease (Roberts et al. in Physiol Plant 118:483-490, 2003) [23].
• Western blot analysis demonstrated that P1 appeared in extracts from non-detached dark-induced senescent leaves but was undetectable in leaves senescing after nitrogen (N) deprivation [23].
• P1 signal was detected at late stages of ethephon or methyl jasmonate-induced senescence but was undetectable in senescent leaves from plants treated with abscisic acid [23].
• We have previously reported the occurrence of two serine endoproteases (referred to as P1 and P2) in dark-induced senescent wheat (Triticum aestivum L.) leaves [23].

Physical interactions of RPLP1

• It is concluded that the heterodimeric complex of the P1/P2 proteins is formed preferentially [24].

Regulatory relationships of RPLP1

• When injected to animals, P1 protein induced only experimental allergic neuritis while P2 protein induced both mild experimental allergic neuritis and experimental allergic encephalomyelitis [21].

Other interactions of RPLP1

• P2 along with its other family members, P0 and P1, constitutes a part of the elongation factor-binding site connected to the GTPase center in the 60S ribosomal subunit [25].
• Further, P2 and P1 are shown to be good in vitro substrates for GRK2 with K(M) values approximating 1 microM [25].
• Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B [15].
• Isolation of the 4 kDa fragment by reversed-phase HPLC, followed by N-terminal amino acid sequencing, demonstrated that the cleavage of alpha 1AT occurred at the Pro357-Met358 (P2-P1) peptide bond, one peptide bond to the N-terminal side of the inhibitory site [26].
• We examined the secretion of MMP9 by primary culture (P0), passage 1 (P1) and passage 2 (P2) human umbilical vein endothelial cells (HUVE) [27].

Analytical, diagnostic and therapeutic context of RPLP1

• Northern blotting analyses showed that mRNAs for P1 and P2 genes had no significant difference in lengths and amounts between control and patient cells [28].
• ELISA with P0, P1 and P2, premixed at equimolar concentrations, gave higher OD readings than each protein tested individually [29].
• The patient's serum produced nucleolar and cytoplasmic staining by indirect immunofluorescence analyses on HEp-2 cell substrate and reacted with P0, P1 and P2 proteins in immunoblotting using purified ribosomal antigens [30].
• Another additional peculiarity in Leishmania will be discussed about of the amino acid divergence rate of three structural proteins: acidic ribosomal P1 and P2b proteins, and histone H3 by using multiple sequence alignment and dendrograms [31].
• P1, P2 proteins and the basic protein of the central nervous system have been shown to have different electrophoretic mobility, and each of the two peripheral basic proteins was shown to be homogeneous by disc electrophoresis [21].

References