The Optional Introns in Yeast Mitochondrial DNA

Author(s):  
P. Borst
1980 ◽  
Vol 255 (24) ◽  
pp. 11922-11926 ◽  
Author(s):  
S.G. Bonitz ◽  
G. Coruzzi ◽  
B.E. Thalenfeld ◽  
A. Tzagoloff ◽  
G. Macino

1988 ◽  
Vol 8 (6) ◽  
pp. 2361-2366 ◽  
Author(s):  
K A Jarrell ◽  
R C Dietrich ◽  
P S Perlman

A self-splicing group II intron of yeast mitochondrial DNA (aI5g) was divided within intron domain 4 to yield two RNAs that trans-spliced in vitro with associated trans-branching of excised intron fragments. Reformation of the domain 4 secondary structure was not necessary for the trans reaction, since domain 4 sequences were shown to be dispensable. Instead, the trans reaction depended on a previously unpredicted interaction between intron domain 5, the most highly conserved region of group II introns, and another region of the RNA. Domain 5 was shown to be essential for cleavage at the 5' splice site. It stimulated that cleavage when supplied as a trans-acting RNA containing only 42 nucleotides of intron sequence. The relevance of our findings to in vivo trans-splicing mechanisms is discussed.


1992 ◽  
Vol 12 (6) ◽  
pp. 2561-2569 ◽  
Author(s):  
L L Stohl ◽  
D A Clayton

Yeast mitochondrial DNA contains multiple promoters that sponsor different levels of transcription. Several promoters are individually located immediately adjacent to presumed origins of replication and have been suggested to play a role in priming of DNA replication. Although yeast mitochondrial DNA replication origins have not been extensively characterized at the primary sequence level, a common feature of these putative origins is the occurrence of a short guanosine-rich region in the priming strand downstream of the transcriptional start site. This situation is reminiscent of vertebrate mitochondrial DNA origins and raises the possibility of common features of origin function. In the case of human and mouse cells, there exists an RNA processing activity with the capacity to cleave at a guanosine-rich mitochondrial RNA sequence at an origin; we therefore sought the existence of a yeast endoribonuclease that had such a specificity. Whole cell and mitochondrial extracts of Saccharomyces cerevisiae contain an RNase that cleaves yeast mitochondrial RNA in a site-specific manner similar to that of the human and mouse RNA processing activity RNase MRP. The exact location of cleavage within yeast mitochondrial RNA corresponds to a mapped site of transition from RNA to DNA synthesis. The yeast activity also cleaved mammalian mitochondrial RNA in a fashion similar to that of the mammalian RNase MRPs. The yeast endonuclease is a ribonucleoprotein, as judged by its sensitivity to nucleases and proteinase, and it was present in yeast strains lacking mitochondrial DNA, which demonstrated that all components required for in vitro cleavage are encoded by nuclear genes. We conclude that this RNase is the yeast RNase MRP.


1984 ◽  
Vol 81 (10) ◽  
pp. 3148-3152 ◽  
Author(s):  
M. E. Hudspeth ◽  
R. D. Vincent ◽  
P. S. Perlman ◽  
D. S. Shumard ◽  
L. O. Treisman ◽  
...  

2008 ◽  
Vol 54 (2) ◽  
pp. 105-109 ◽  
Author(s):  
Matus Valach ◽  
Lubomir Tomaska ◽  
Jozef Nosek

Author(s):  
H.F. Tabak ◽  
K.A. Osinga ◽  
E. de Vries ◽  
A.M. van der Bliek ◽  
G.T.J. van der Horst ◽  
...  

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