II. Yeast sequencing reports. The sequence of an 8·8 kb segment on the left arm of chromosome II fromSaccharomyces cerevisiae reveals four new open reading frames including homologs of animal DNA polymerase α-primases and bacterial GTP cyclohydrolase II

Yeast ◽  
1994 ◽  
Vol 10 (S1994A) ◽  
pp. S13-S24 ◽  
Author(s):  
Luc van Dyck ◽  
Bénédicte Purnelle ◽  
André Goffeau ◽  
Jacek Skala
1998 ◽  
Vol 180 (8) ◽  
pp. 2232-2236 ◽  
Author(s):  
Yoshizumi Ishino ◽  
Kayoko Komori ◽  
Isaac K. O. Cann ◽  
Yosuke Koga

ABSTRACT One of the most puzzling results from the complete genome sequence of the methanogenic archaeon Methanococcus jannaschii was that the organism may have only one DNA polymerase gene. This is because no other DNA polymerase-like open reading frames (ORFs) were found besides one ORF having the typical α-like DNA polymerase (family B). Recently, we identified the genes of DNA polymerase II (the second DNA polymerase) from the hyperthermophilic archaeonPyrococcus furiosus, which has also at least one α-like DNA polymerase (T. Uemori, Y. Sato, I. Kato, H. Doi, and Y. Ishino, Genes Cells 2:499–512, 1997). The genes in M. jannaschiiencoding the proteins that are homologous to the DNA polymerase II ofP. furiosus have been located and cloned. The gene products of M. jannaschii expressed in Escherichia colihad both DNA polymerizing and 3′→5′ exonuclease activities. We propose here a novel DNA polymerase family which is entirely different from other hitherto-described DNA polymerases.


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

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

1994 ◽  
Vol 302 (1) ◽  
pp. 215-221 ◽  
Author(s):  
M Gütlich ◽  
E Jaeger ◽  
K P Rücknagel ◽  
T Werner ◽  
W Rödl ◽  
...  

GTP cyclohydrolase I catalyses the first and rate-limiting step of tetrahydrobiopterin biosynthesis. Its expression is regulated by interferon-gamma or kit ligand in a tissue-specific manner. Three different cDNA forms have been reported for human GTP cyclohydrolase I [Togari, Ichinose, Matsumoto, Fujita and Nagatsu (1992) Biochem. Biophys. Res. Commun. 187, 359-365]. We have isolated, from a human liver cDNA library, two clones which contained inserts identical with two of the cDNAs reported by Togari et al. (1992). The three open reading frames corresponding to all reported cDNA sequences were expressed in Escherichia coli. Only the recombinant protein corresponding to the longest reading frame catalysed the conversion of GTP into dihydroneopterin triphosphate. The proteins corresponding to the shorter reading frames failed to catalyse not only the generation of dihydroneopterin triphosphate but also the release of formate from GTP, an intermediate step of the reaction. Recombinant human GTP cyclohydrolase I showed sigmoidal substrate kinetics and maximum activity at 60 degrees C. These findings are well in line with the published properties of the enzyme isolated from rat liver. The data indicate that cytokine-mediated induction of GTP cyclohydrolase I is not due to the expression of enzyme isoforms.


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

Yeast ◽  
1993 ◽  
Vol 9 (3) ◽  
pp. 289-293 ◽  
Author(s):  
Axel Baur ◽  
Ine Schaaff-Gerstenschläger ◽  
Eckhard Boles ◽  
Thomas Miosga ◽  
Matthias Rose ◽  
...  

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