60S acidic ribosomal protein P1 explained

60S acidic ribosomal protein P1 is a protein that in humans is encoded by the RPLP1 gene.^[1]

Function

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal phosphoprotein that is a component of the 60S subunit. The protein, which is a functional equivalent of the Escherichia coli L7/L12 ribosomal protein, belongs to the L12P family of ribosomal proteins. It plays an important role in the elongation step of protein synthesis. Unlike most ribosomal proteins, which are basic, the encoded protein is acidic. Its C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1 protein can interact with P0 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Two alternatively spliced transcript variants that encode different proteins have been observed. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.^[1]

Interactions

RPLP1 has been shown to interact with RPLP2.^[2]

References

Further reading

• Wool IG, Chan YL, Glück A . Structure and evolution of mammalian ribosomal proteins . Biochemistry and Cell Biology . 73 . 11–12 . 933–47 . 1996 . 8722009 . 10.1139/o95-101 .
• Rich BE, Steitz JA . Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly . Molecular and Cellular Biology . 7 . 11 . 4065–74 . November 1987 . 3323886 . 368077 . 10.1128/mcb.7.11.4065.
• Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T . Construction of a human full-length cDNA bank . Gene . 150 . 2 . 243–50 . December 1994 . 7821789 . 10.1016/0378-1119(94)90433-2 .
• Tchórzewski M, Boldyreff B, Issinger OG, Grankowski N . Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: evaluation by the two hybrid system . The International Journal of Biochemistry & Cell Biology . 32 . 7 . 737–46 . July 2000 . 10856704 . 10.1016/S1357-2725(00)00017-0 .
• Chan SH, Hung FS, Chan DS, Shaw PC . Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B . European Journal of Biochemistry . 268 . 7 . 2107–12 . April 2001 . 11277934 . 10.1046/j.1432-1327.2001.02091.x . free .
• Uechi T, Tanaka T, Kenmochi N . A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders . Genomics . 72 . 3 . 223–30 . March 2001 . 11401437 . 10.1006/geno.2000.6470 .
• Yoshihama M, Uechi T, Asakawa S, Kawasaki K, Kato S, Higa S, Maeda N, Minoshima S, Tanaka T, Shimizu N, Kenmochi N . The human ribosomal protein genes: sequencing and comparative analysis of 73 genes . Genome Research . 12 . 3 . 379–90 . March 2002 . 11875025 . 155282 . 10.1101/gr.214202 .
• Kang MJ, Ahn HS, Lee JY, Matsuhashi S, Park WY . Up-regulation of PDCD4 in senescent human diploid fibroblasts . Biochemical and Biophysical Research Communications . 293 . 1 . 617–21 . April 2002 . 12054647 . 10.1016/S0006-291X(02)00264-4 .
• Tchórzewski M, Krokowski D, Rzeski W, Issinger OG, Grankowski N . The subcellular distribution of the human ribosomal "stalk" components: P1, P2 and P0 proteins . The International Journal of Biochemistry & Cell Biology . 35 . 2 . 203–11 . February 2003 . 12479870 . 10.1016/S1357-2725(02)00133-4 .
• Shu H, Chen S, Bi Q, Mumby M, Brekken DL . Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line . Molecular & Cellular Proteomics . 3 . 3 . 279–86 . March 2004 . 14729942 . 10.1074/mcp.D300003-MCP200 . free .
• Giorgianni F, Beranova-Giorgianni S, Desiderio DM . Identification and characterization of phosphorylated proteins in the human pituitary . Proteomics . 4 . 3 . 587–98 . March 2004 . 14997482 . 10.1002/pmic.200300584 . 25355914 .
• Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R . Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry . Nature Methods . 2 . 8 . 591–8 . August 2005 . 16094384 . 10.1038/nmeth776 . 20475874 .
• Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J . Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC . Proteomics . 5 . 14 . 3589–99 . September 2005 . 16097034 . 10.1002/pmic.200401217 . 895879 .
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE . A human protein-protein interaction network: a resource for annotating the proteome . Cell . 122 . 6 . 957–68 . September 2005 . 16169070 . 10.1016/j.cell.2005.08.029 . 11858/00-001M-0000-0010-8592-0 . 8235923 . free .
• Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R . Phosphoproteome analysis of the human mitotic spindle . Proceedings of the National Academy of Sciences of the United States of America . 103 . 14 . 5391–6 . April 2006 . 16565220 . 1459365 . 10.1073/pnas.0507066103 . 2006PNAS..103.5391N . free .
• Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F . Phosphoproteomic analysis of the human pituitary . Pituitary . 9 . 2 . 109–20 . 2006 . 16807684 . 10.1007/s11102-006-8916-x . 10789246 .

Notes and References

1. Web site: Entrez Gene: RPLP1 ribosomal protein, large, P1.
2. Tchórzewski M, Boldyreff B, Issinger OG, Grankowski N . Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: evaluation by the two hybrid system . The International Journal of Biochemistry & Cell Biology . 32 . 7 . 737–46 . July 2000 . 10856704 . 10.1016/S1357-2725(00)00017-0 .