Sequence and function analysis of a 4·3 kb fragment ofSaccharomyces cerevisiae chromosome II including three open reading frames

Yeast ◽  
1993 ◽  
Vol 9 (8) ◽  
pp. 915-921 ◽  
Author(s):  
Ine Schaaff-Gerstenschläger ◽  
Axel Baur ◽  
Eckhard Boles ◽  
Friedrich K. Zimmermann
Yeast ◽  
1994 ◽  
Vol 10 (9) ◽  
pp. 1257-1257
Author(s):  
Ine Schaaff-Gerstenschläger ◽  
Axel Baur ◽  
Eckhard Boles ◽  
Friedrich K. Zimmermann

Yeast ◽  
1993 ◽  
Vol 9 (12) ◽  
pp. 1355-1371 ◽  
Author(s):  
Bart Scherens ◽  
Mohamed El Bakkoury ◽  
Fabienne Vierendeels ◽  
Evelyne Dubois ◽  
Francine Messenguy

Yeast ◽  
1993 ◽  
Vol 9 (11) ◽  
pp. 1273-1277 ◽  
Author(s):  
Thomas Miosga ◽  
Friedrich K. Zimmermann

2015 ◽  
Vol 2015 ◽  
pp. 1-5 ◽  
Author(s):  
Vladimir Egorov ◽  
Natalia Grudinina ◽  
Andrey Vasin ◽  
Dmitry Lebedev

Changes in protein conformation can occur both as part of normal protein functioning and during disease pathogenesis. The most common conformational diseases are amyloidoses. Sometimes the development of a number of diseases which are not traditionally related to amyloidoses is associated with amyloid-like conformational transitions of proteins. Also, amyloid-like aggregates take part in normal physiological processes such as memorization and cell signaling. Several primary structural features of a protein are involved in conformational transitions. Also the protein proteolytic fragments can cause the conformational transitions in the protein. Short peptides which could be produced during the protein life cycle or which are encoded by short open reading frames can affect the protein conformation and function.


Yeast ◽  
1995 ◽  
Vol 11 (5) ◽  
pp. 455-458 ◽  
Author(s):  
Sabine Baur ◽  
Jûrgen Becker ◽  
Ziyu Li ◽  
Eckhard Niegemann ◽  
Eugen Wehner ◽  
...  

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e8356
Author(s):  
Darrin T. Schultz ◽  
Jordan M. Eizenga ◽  
Russell B. Corbett-Detig ◽  
Warren R. Francis ◽  
Lynne M. Christianson ◽  
...  

To date, five ctenophore species’ mitochondrial genomes have been sequenced, and each contains open reading frames (ORFs) that if translated have no identifiable orthologs. ORFs with no identifiable orthologs are called unidentified reading frames (URFs). If truly protein-coding, ctenophore mitochondrial URFs represent a little understood path in early-diverging metazoan mitochondrial evolution and metabolism. We sequenced and annotated the mitochondrial genomes of three individuals of the beroid ctenophore Beroe forskalii and found that in addition to sharing the same canonical mitochondrial genes as other ctenophores, the B. forskalii mitochondrial genome contains two URFs. These URFs are conserved among the three individuals but not found in other sequenced species. We developed computational tools called pauvre and cuttlery to determine the likelihood that URFs are protein coding. There is evidence that the two URFs are under negative selection, and a novel Bayesian hypothesis test of trinucleotide frequency shows that the URFs are more similar to known coding genes than noncoding intergenic sequence. Protein structure and function prediction of all ctenophore URFs suggests that they all code for transmembrane transport proteins. These findings, along with the presence of URFs in other sequenced ctenophore mitochondrial genomes, suggest that ctenophores may have uncharacterized transmembrane proteins present in their mitochondria.


Yeast ◽  
1994 ◽  
Vol 10 (1) ◽  
pp. 131-131 ◽  
Author(s):  
Axel Baur ◽  
Ine Schaaff-Gerstenschläger ◽  
Eckhard Boles ◽  
Thomas Miosga ◽  
Matthias Rose ◽  
...  

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