Euglena gracilis chloroplast ribosomal RNA transcription units. II. Nucleotide sequence homology between the 16 S–23 S ribosomal RNA spacer and the 16 S ribosomal RNA leader regions.
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چکیده
منابع مشابه
Nucleotide Sequence Homology Exists between the Chloroplast and Nuclear Ribosomal DNAs of Euglena gracilis.
The nuclear and chloroplast ribosomal DNAs from Euglena were shown to have specific regions of nucleotide sequence homology. The regions of homology were identified by hybridization of restriction endonuclease DNA fragments of cloned chloroplast and nuclear ribosomal DNAs to one another. The regions of homology between these two ribosomal DNAs were in that part of the genes that code for the 3'...
متن کاملCharacterization of a Euglena gracilis chloroplast RNA polymerase specific for ribosomal RNA genes.
Euglena gracilis chloroplasts contain a 145,000-base pair chromosome that encodes genes for ribosomal, transfer, and messenger RNAs. These genes are transcribed within the organelle by chloroplast RNA polymerase activities that are specific for different classes of RNA. Two transcriptional activities have been isolated from Euglena chloroplasts. (Greenberg, B. M., Narita, J. O., DeLuca-Flaherty...
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The human rDNA tandem repeat consists of 13.3 kb of transcribed sequence and about 30 kb of intergenic spacer of unknown function. For descriptive purposes, it is convenient to divide the ribosomal repeat into 4 EcoRI fragments, A D . The C fragment contains only intergenic spacer sequences, and ends some 500 bp upstream of the ribosomal RNA promoter. We had previously described the terminal Ba...
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A secondary structure model for 16S ribosomal RNA which is based on available chemical, enzymatic, and comparative sequence data shows good agreement between constraints dictated by the model and a wide variety of experimental observations. The four major structural domains created by the base-pairing scheme correspond closely to RNA fragments isolated after nuclease digestion in the presence o...
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In bacteria, the expression of ribosomal proteins is often feedback-regulated at the translational level by the binding of the protein to its own mRNA. This is the case for L20, which binds to two distinct sites of its mRNA that both resemble its binding site on 23 S rRNA. In the present work, we report an NMR analysis of the interaction between the C-terminal domain of L20 (L20C) and both its ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)70406-2