Conţinutul numărului revistei |
Articolul precedent |
Articolul urmator |
282 0 |
Căutarea după subiecte similare conform CZU |
577.218 (5) |
Material bases of life. Biochemistry. Molecular biology. Biophysics (668) |
SM ISO690:2012 PAZ, Arnon, MESTER, David, BACA, Ivan, NEVO, Eviatar N., KOROL, Abraham B.. Adaptive role of increase frequency of polypurine tracts in mRNA sequences of thermophilic prokaryotes. In: Proceedings of the National Academy of Sciences of the United States of America, 2004, vol. 101, pp. 2951-2956. ISSN 0027-8424. DOI: https://doi.org/10.1073/pnas.0308594100 |
EXPORT metadate: Google Scholar Crossref CERIF DataCite Dublin Core |
Proceedings of the National Academy of Sciences of the United States of America | ||||||
Volumul 101 / 2004 / ISSN 0027-8424 /ISSNe 1091-6490 | ||||||
|
||||||
DOI:https://doi.org/10.1073/pnas.0308594100 | ||||||
CZU: 577.218 | ||||||
Pag. 2951-2956 | ||||||
|
||||||
Rezumat | ||||||
The mechanism of an organism's adaptation to high temperatures has been investigated intensively in recent years. It was suggested that the macromolecules of thermophilic microorganisms (especially proteins) have structural features that enhance their thermostability. We compared mRNA sequences of 72 fully sequenced prokaryotic proteomes (14 thermophilic and 58 mesophilic species). Although the differences between the percentage of adenine plus guanine content of whole mRNAs of different prokaryotic species are much lower than those of guanine plus cytosine content, the thermophile purine-pyrimidine (R/Y) ratio within their mRNAs is significantly higher than that of the mesophiles. The first and third codon positions of both thermophiles and mesophiles are purine-biased, with the bias more pronounced by the thermophiles. Thermophile mRNAs that display the highest R/Y ratio (1.43-1.69) are those of the ribosomal proteins, histone-like proteins, DNA-dependent RNA polymerase subunits, and heat-shock proteins. Within mesophilic prokaryotes and five eukaryotic species, the R/Y ratio of the mRNAs of heat-shock proteins is higher than their average over coding part of the genome. Polypurine tracts (R)n (with n ≥ 5) are much more abundant within the thermophile mRNAs compared with mesophiles. Between two sequential pure-purinic codons of thermophile mRNAs, there is a rather strong tendency for the occurrence of adenine but not guanine tracts. The data suggest that mixed adenine-guanine and polyadenine tracts in mRNAs increase the thermostability beyond the contribution of amino acids encoded by purine tracts, which highlights the importance of ecological stress in the evolution of genome architecture. |
||||||
Cuvinte-cheie MeSH Animals, Arabidopsis, archaea, Bacteria, Base Sequence, DNA-Directed RNA Polymerases, Drosophila melanogaster, heat, histones, kinetics, Oryza sativa, Plasmodium falciparum, Prokaryotic Cells, Purines, Ribosomal Proteins, RNA, Messenger, thermodynamics, transcription, Genetic Species Index Bacteria (microorganisms), Eukaryota, Prokaryota EMTREE drug terms heat shock protein, purine, DNA directed RNA polymerase, histone, messenger RNA, purine derivative, ribosome protein EMTREE medical terms adaptation, article, Codon, frequency analysis, genome analysis, macromolecule, messenger RNA synthesis, nonhuman, priority journal, prokaryote, Protein content, protein structure, RNA sequence, species differentiation, thermophilic bacterium, thermostability, animal, Arabidopsis, Archaebacterium, bacterium, Chemistry, Drosophila melanogaster, genetic transcription, genetics, heat, kinetics, nucleotide sequence, physiology, Plasmodium falciparum, prokaryotic cell, rice, thermodynamics |
||||||
|
DataCite XML Export
<?xml version='1.0' encoding='utf-8'?> <resource xmlns:xsi='http://www.w3.org/2001/XMLSchema-instance' xmlns='http://datacite.org/schema/kernel-3' xsi:schemaLocation='http://datacite.org/schema/kernel-3 http://schema.datacite.org/meta/kernel-3/metadata.xsd'> <identifier identifierType='DOI'>10.1073/pnas.0308594100</identifier> <creators> <creator> <creatorName>Paz, A.</creatorName> <affiliation>Institute of Evolution, University of Haifa, Israel</affiliation> </creator> <creator> <creatorName>Mester, D.</creatorName> <affiliation>Institute of Evolution, University of Haifa, Israel</affiliation> </creator> <creator> <creatorName>Baca, I.</creatorName> <affiliation>Institute of Evolution, University of Haifa, Israel</affiliation> </creator> <creator> <creatorName>Nevo, E.</creatorName> <affiliation>Institute of Evolution, University of Haifa, Israel</affiliation> </creator> <creator> <creatorName>Korol, A.</creatorName> <affiliation>Institute of Evolution, University of Haifa, Israel</affiliation> </creator> </creators> <titles> <title xml:lang='en'>Adaptive role of increase frequency of polypurine tracts in mRNA sequences of thermophilic prokaryotes</title> </titles> <publisher>Instrumentul Bibliometric National</publisher> <publicationYear>2004</publicationYear> <relatedIdentifier relatedIdentifierType='ISSN' relationType='IsPartOf'>0027-8424</relatedIdentifier> <subjects> <subject>MeSH Animals</subject> <subject>Arabidopsis</subject> <subject>archaea</subject> <subject>Bacteria</subject> <subject>Base Sequence</subject> <subject>DNA-Directed RNA Polymerases</subject> <subject>Drosophila melanogaster</subject> <subject>heat</subject> <subject>histones</subject> <subject>kinetics</subject> <subject>Oryza sativa</subject> <subject>Plasmodium falciparum</subject> <subject>Prokaryotic Cells</subject> <subject>Purines</subject> <subject>Ribosomal Proteins</subject> <subject>RNA</subject> <subject>Messenger</subject> <subject>thermodynamics</subject> <subject>transcription</subject> <subject>Genetic Species Index Bacteria (microorganisms)</subject> <subject>Eukaryota</subject> <subject>Prokaryota EMTREE drug terms heat shock protein</subject> <subject>purine</subject> <subject>DNA directed RNA polymerase</subject> <subject>histone</subject> <subject>messenger RNA</subject> <subject>purine derivative</subject> <subject>ribosome protein EMTREE medical terms adaptation</subject> <subject>article</subject> <subject>Codon</subject> <subject>frequency analysis</subject> <subject>genome analysis</subject> <subject>macromolecule</subject> <subject>messenger RNA synthesis</subject> <subject>nonhuman</subject> <subject>priority journal</subject> <subject>prokaryote</subject> <subject>Protein content</subject> <subject>protein structure</subject> <subject>RNA sequence</subject> <subject>species differentiation</subject> <subject>thermophilic bacterium</subject> <subject>thermostability</subject> <subject>animal</subject> <subject>Arabidopsis</subject> <subject>Archaebacterium</subject> <subject>bacterium</subject> <subject>Chemistry</subject> <subject>Drosophila melanogaster</subject> <subject>genetic transcription</subject> <subject>genetics</subject> <subject>heat</subject> <subject>kinetics</subject> <subject>nucleotide sequence</subject> <subject>physiology</subject> <subject>Plasmodium falciparum</subject> <subject>prokaryotic cell</subject> <subject>rice</subject> <subject>thermodynamics</subject> <subject schemeURI='http://udcdata.info/' subjectScheme='UDC'>577.218</subject> </subjects> <dates> <date dateType='Issued'>2004-03-02</date> </dates> <resourceType resourceTypeGeneral='Text'>Journal article</resourceType> <descriptions> <description xml:lang='en' descriptionType='Abstract'><p>The mechanism of an organism's adaptation to high temperatures has been investigated intensively in recent years. It was suggested that the macromolecules of thermophilic microorganisms (especially proteins) have structural features that enhance their thermostability. We compared mRNA sequences of 72 fully sequenced prokaryotic proteomes (14 thermophilic and 58 mesophilic species). Although the differences between the percentage of adenine plus guanine content of whole mRNAs of different prokaryotic species are much lower than those of guanine plus cytosine content, the thermophile purine-pyrimidine (R/Y) ratio within their mRNAs is significantly higher than that of the mesophiles. The first and third codon positions of both thermophiles and mesophiles are purine-biased, with the bias more pronounced by the thermophiles. Thermophile mRNAs that display the highest R/Y ratio (1.43-1.69) are those of the ribosomal proteins, histone-like proteins, DNA-dependent RNA polymerase subunits, and heat-shock proteins. Within mesophilic prokaryotes and five eukaryotic species, the R/Y ratio of the mRNAs of heat-shock proteins is higher than their average over coding part of the genome. Polypurine tracts (R)<sub>n</sub> (with n ≥ 5) are much more abundant within the thermophile mRNAs compared with mesophiles. Between two sequential pure-purinic codons of thermophile mRNAs, there is a rather strong tendency for the occurrence of adenine but not guanine tracts. The data suggest that mixed adenine-guanine and polyadenine tracts in mRNAs increase the thermostability beyond the contribution of amino acids encoded by purine tracts, which highlights the importance of ecological stress in the evolution of genome architecture.</p></description> </descriptions> <formats> <format>application/pdf</format> </formats> </resource>