GLORIA

GEOMAR Library Ocean Research Information Access

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    The use of ribonuclease U2 in RNA sequence determination (1974)
    Springer
    Journal of molecular evolution 3 (1974), S. 63-77 
    Details
    ISSN: 1432-1432
    Keywords: 16S Ribosomal RNA ; Oligonucleotide ; Fingerprint ; Ribonuclease U2 ; Escherichia coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The catalog of oligomers produced by ribonuclease T1 digestion ofEscherichi coli 16S ribosomal RNA has been determined by a new method that involves the use of ribonuclease U2 fromUstilago sphaerogena. The sequences for the larger T1 oligomers (8 or more bases) determined in this way differ in more than 50 % of the cases from those reported previously (determined by other methods).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01795977
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Evidence for Heterogeneity of 23 S RNA in E. coli (1969)
    [s.l.] : Nature Publishing Group
    Nature 221 (1969), S. 864-865 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Total RNA was isolated from E. coli (15 TAU?) by a variation of the method of Hayashi and Spiegelman5. 23S RNA was isolated on a Beckman L-4 zonal ultra-centrifuge as described by Hastings et al.6. After precipitation from the sucrose density gradient (RNase free sucrose?Schwarz Biochem.) the RNA ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/221864a0
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Molecular interactions of ribosomal components (1970)
    Springer
    Molecular genetics and genomics 109 (1970), S. 193-205 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The formation of a complex between individual 30S ribosomal proteins and 16S ribosomal RNA was studied by three techniques: zone centrifugation, molecular-sieve chromatography and electrophoresis in polyacrylamide gels. Five 30S proteins form a stable complex with the RNA under the conditions used to assemble ribosomes. Specific and nonspecific complex formation can be distinguished by an analysis of the concentration-dependence for complex formation. Similarly, competition experiments between heterologous proteins that bind to RNA can also be used to establish the uniquness of the RNA binding sites for ribosomal proteins. The data show that four of the five proteins bind to unique sites on the RNA. The fifth protein binds nonspecifically to the RNA. In addition, cooperative interactions between several proteins were observed; these enhance the interaction of proteins with the 16S RNA. A partial assembly sequence for the 30S ribosomal subunit is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267007
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Molecular interactions of ribosomal components (1971)
    Springer
    Molecular genetics and genomics 112 (1971), S. 1-8 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Five of the 30S ribosomal proteins from E. coli were tested for their ability to bind to 16S ribosomal RNA. Only one of these, S15, can form a complex with the RNA. Quantitative measurements as well as competition experiments show that the RNA binding site for the attachment of S15 is specific for this protein. These experiments complete our analysis of all 21 of the 30S ribosomal proteins. Five of these have now been shown to form a site-specific complex with 16S RNA. These are S4, S7, S8, S15 and S20. The relationship of these data to the assembly and structure of the ribosome are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266926
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Characterization of an RNA “binding site” for a specific ribosomal protein of Escherichia coli (1972)
    Springer
    Molecular genetics and genomics 114 (1972), S. 1-8 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A portion of the 16S ribosomal RNA that binds specifically to, and is protected from nucleolytic attack by, ribosomal protein S4 has been characterized in terms of its partial primary structure. The specific RNA (S4aR) in question comprises slightly more than onefourth of the full 16S molecule, and appears to be located (at least in part) in the 5′-proximal half of the molecule. The functional significance of S4aR is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268740
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Molecular interactions of ribosomal components (1972)
    Springer
    Molecular genetics and genomics 114 (1972), S. 350-357 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The site-specific complex formed between 16S RNA and the 30S ribosomal protein S4 from Escherichia coli has been degraded with pancreatic ribonuclease. We have recovered the nuclease-resistant RNA from this complex; we call it S4aR. S4aR will bind to S4, but it will not bind to the other 30S proteins that can form site-specific complexes with 16S RNA. The data presented here as well as elsewhere (Schaup et al., 1971b) show that S4aR has a mass of about 150000 daltons and that it is made up of several separate RNA fragments, each of which enters the complex with S4. We conclude that S4 interacts with several separate binding sites on the RNA and that these probably contain a great deal of double stranded structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267503
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...