Mammalian ribosomal protein (rp) genes are members of multigene families which are composed predominantly of multiple processed pseudogenes and one functional intron-containing gene. The presence of multiple pseudogenes has hampered the isolation and study of the functional rp genes. We have recently developed a polymerase chain reaction (PCR)-based strategy for the detection of intron-containing genes in the presence of multiple pseudogenes (B. Davies, S. Feo, E. Heard, and M. Fried, 1989, Proc. Natl. Acad. Sci. USA 86: 6691-6695). We have used this technique to identify the intron-containing PCR products of seven human rp genes (rpL19, rpL30, rpL35a, rpL36a, rpS6, rpS11, rpS17) and to map their chromosomal locations. No linkage was found between any of these seven rp genes nor was linkage found to the three other rp genes previously mapped. The wide distribution of the rp genes throughout the human genome strongly suggests that the coordinate regulation of the expression of mammalian ribosomal proteins in response to the cell's varying requirements for protein synthesis is not a result of cis activation of chromosomal regions but is mediated by trans-acting factors.
Mammalian ribosomal protein (rp) genes are members of multigene families which are composed predominantly of multiple processed pseudogenes and one functional intron-containing gene. The presence of multiple pseudogenes has hampered the isolation and study of the functional rp genes. We have recently developed a polymerase chain reaction (PCR)-based strategy for the detection of intron-containing genes in the presence of multiple pseudogenes (B. Davies, S. Feo, E. Heard, and M. Fried, 1989, Proc. Natl. Acad. Sci. USA 86: 6691-6695). We have used this technique to identify the intron-containing PCR products of seven human rp genes (rpL19, rpL30, rpL35a, rpL36a, rpS6, rpS11, rpS17) and to map their chromosomal locations. No linkage was found between any of these seven rp genes nor was linkage found to the three other rp genes previously mapped. The wide distribution of the rp genes throughout the human genome strongly suggests that the coordinate regulation of the expression of mammalian ribosomal proteins in response to the cell's varying requirements for protein synthesis is not a result of cis activation of chromosomal regions but is mediated by trans-acting factors.
J. Protein Chem. 22, 249-258 (2003)[PubMed:12962325]
The 60S ribosomal proteins were isolated from ribosomes of human placenta and separated by reversed phase HPLC. The fractions obtained were subjected to trypsin and Glu-C digestion and analyzed by mass fingerprinting (MALDI-TOF), MS/MS (ESI), and Edman sequencing. Forty-six large subunit proteins were found, 22 of which showed masses in accordance with the SwissProt database (June 2002) masses (proteins L6, L7, L9, L13, L15, L17, L18, L21, L22, L24, L26, L27, L30, L32, L34, L35, L36, L37, L37A, L38, L39, L41). Eleven (proteins L7, L10A, L11, L12, L13A, L23, L23A, L27A, L28, L29, and P0) resulted in mass changes that are consistent with N-terminal loss of methionine, acetylation, internal methylation, or hydroxylation. A loss of methionine without acetylation was found for protein L8 and L17. For nine proteins (L3, L4, L5, L7A, L10, L14, L19, L31, and L40), the molecular masses could not be determined. Proteins P1 and protein L3-like were not identified by the methods applied.
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA. Translation ends with the release of a polypeptide chain from the ribosome.
Mammalian ribosomal protein (rp) genes are members of multigene families which are composed predominantly of multiple processed pseudogenes and one functional intron-containing gene. The presence of multiple pseudogenes has hampered the isolation and study of the functional rp genes. We have recently developed a polymerase chain reaction (PCR)-based strategy for the detection of intron-containing genes in the presence of multiple pseudogenes (B. Davies, S. Feo, E. Heard, and M. Fried, 1989, Proc. Natl. Acad. Sci. USA 86: 6691-6695). We have used this technique to identify the intron-containing PCR products of seven human rp genes (rpL19, rpL30, rpL35a, rpL36a, rpS6, rpS11, rpS17) and to map their chromosomal locations. No linkage was found between any of these seven rp genes nor was linkage found to the three other rp genes previously mapped. The wide distribution of the rp genes throughout the human genome strongly suggests that the coordinate regulation of the expression of mammalian ribosomal proteins in response to the cell's varying requirements for protein synthesis is not a result of cis activation of chromosomal regions but is mediated by trans-acting factors.
J. Protein Chem. 22, 249-258 (2003)[PubMed:12962325]
The 60S ribosomal proteins were isolated from ribosomes of human placenta and separated by reversed phase HPLC. The fractions obtained were subjected to trypsin and Glu-C digestion and analyzed by mass fingerprinting (MALDI-TOF), MS/MS (ESI), and Edman sequencing. Forty-six large subunit proteins were found, 22 of which showed masses in accordance with the SwissProt database (June 2002) masses (proteins L6, L7, L9, L13, L15, L17, L18, L21, L22, L24, L26, L27, L30, L32, L34, L35, L36, L37, L37A, L38, L39, L41). Eleven (proteins L7, L10A, L11, L12, L13A, L23, L23A, L27A, L28, L29, and P0) resulted in mass changes that are consistent with N-terminal loss of methionine, acetylation, internal methylation, or hydroxylation. A loss of methionine without acetylation was found for protein L8 and L17. For nine proteins (L3, L4, L5, L7A, L10, L14, L19, L31, and L40), the molecular masses could not be determined. Proteins P1 and protein L3-like were not identified by the methods applied.
Proteins conjugated with ribonucleic acid (RNA). Ribonucleoprotein are involved in a wide range of cellular processes. Besides ribosomes, in eukaryotic cells both initial RNA transcripts in the nucleus (hnRNA) and cytoplasmic mRNAs exist as complexes with specific sets of proteins. Processing (splicing) of the former is carried out by small nuclear RNPs (snRNPs). Other examples are the signal recognition particle responsible for targetting proteins to endoplasmic reticulum and a complex involved in termination of transcription.
Protein of the ribosome, large ribonucleoprotein particles where the translation of messenger RNA (mRNA) into protein occurs. They are both free in the cytoplasm and attached to membranes of eukaryotic and prokaryotic cells. Ribosomes are also present in all plastids and mitochondria, where they translate organelle-encoded mRNA.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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