Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21

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Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21. / Rosendahl, G; Andreasen, P H; Kristiansen, K.

In: Gene, Vol. 98, No. 2, 1991, p. 161-7.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Rosendahl, G, Andreasen, PH & Kristiansen, K 1991, 'Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21', Gene, vol. 98, no. 2, pp. 161-7. <http://www.ncbi.nlm.nih.gov/pubmed/2016059>

APA

Rosendahl, G., Andreasen, P. H., & Kristiansen, K. (1991). Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21. Gene, 98(2), 161-7. http://www.ncbi.nlm.nih.gov/pubmed/2016059

Vancouver

Rosendahl G, Andreasen PH, Kristiansen K. Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21. Gene. 1991;98(2):161-7.

Author

Rosendahl, G ; Andreasen, P H ; Kristiansen, K. / Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21. In: Gene. 1991 ; Vol. 98, No. 2. pp. 161-7.

Bibtex

@article{abd1935013c411de8478000ea68e967b,
title = "Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21",
abstract = "The single-copy gene encoding ribosomal protein (r-protein) L21 in the macronucleus of the ciliate Tetrahymena thermophila was cloned and characterized. Sequencing of the L21 gene and a corresponding cDNA clone showed the gene to contain three introns, all located in the 3' half of the coding region. Primer extension and nuclease protection analyses revealed five transcription start points (tsp) 56-73 nucleotides upstream from the start codon. The uppermost tsp mapped to the first T in a sequence, TATAA, often found at tsp in T. thermophila. A comparison of amino acid sequences of r-proteins revealed that T. thermophila L21 belongs to a family of r-proteins that have been conserved in eubacteria, archaebacteria and eukaryotes. On the basis of structural and functional considerations, we suggest that the eukaryotic, like the prokaryotic, members of this protein family interact with the 5S RNA complex in ribosomes.",
author = "G Rosendahl and Andreasen, {P H} and K Kristiansen",
note = "Keywords: Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; DNA, Ribosomal; Evolution; Genes; Introns; Molecular Sequence Data; Multigene Family; RNA, Messenger; Restriction Mapping; Ribosomal Proteins; Sequence Homology, Nucleic Acid; Tetrahymena; Transcription, Genetic",
year = "1991",
language = "English",
volume = "98",
pages = "161--7",
journal = "Gene",
issn = "0378-1119",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21

AU - Rosendahl, G

AU - Andreasen, P H

AU - Kristiansen, K

N1 - Keywords: Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; DNA, Ribosomal; Evolution; Genes; Introns; Molecular Sequence Data; Multigene Family; RNA, Messenger; Restriction Mapping; Ribosomal Proteins; Sequence Homology, Nucleic Acid; Tetrahymena; Transcription, Genetic

PY - 1991

Y1 - 1991

N2 - The single-copy gene encoding ribosomal protein (r-protein) L21 in the macronucleus of the ciliate Tetrahymena thermophila was cloned and characterized. Sequencing of the L21 gene and a corresponding cDNA clone showed the gene to contain three introns, all located in the 3' half of the coding region. Primer extension and nuclease protection analyses revealed five transcription start points (tsp) 56-73 nucleotides upstream from the start codon. The uppermost tsp mapped to the first T in a sequence, TATAA, often found at tsp in T. thermophila. A comparison of amino acid sequences of r-proteins revealed that T. thermophila L21 belongs to a family of r-proteins that have been conserved in eubacteria, archaebacteria and eukaryotes. On the basis of structural and functional considerations, we suggest that the eukaryotic, like the prokaryotic, members of this protein family interact with the 5S RNA complex in ribosomes.

AB - The single-copy gene encoding ribosomal protein (r-protein) L21 in the macronucleus of the ciliate Tetrahymena thermophila was cloned and characterized. Sequencing of the L21 gene and a corresponding cDNA clone showed the gene to contain three introns, all located in the 3' half of the coding region. Primer extension and nuclease protection analyses revealed five transcription start points (tsp) 56-73 nucleotides upstream from the start codon. The uppermost tsp mapped to the first T in a sequence, TATAA, often found at tsp in T. thermophila. A comparison of amino acid sequences of r-proteins revealed that T. thermophila L21 belongs to a family of r-proteins that have been conserved in eubacteria, archaebacteria and eukaryotes. On the basis of structural and functional considerations, we suggest that the eukaryotic, like the prokaryotic, members of this protein family interact with the 5S RNA complex in ribosomes.

M3 - Journal article

C2 - 2016059

VL - 98

SP - 161

EP - 167

JO - Gene

JF - Gene

SN - 0378-1119

IS - 2

ER -

ID: 11368384