Structural Studies of the Final Enzyme in the α-Aminoadipate Pathway-Saccharopine Dehydrogenase from Saccharomyces cerevisiae

2007 ◽  
Vol 373 (3) ◽  
pp. 745-754 ◽  
Author(s):  
D.L. Burk ◽  
J. Hwang ◽  
E. Kwok ◽  
L. Marrone ◽  
V. Goodfellow ◽  
...  
Genetics ◽  
2000 ◽  
Vol 156 (3) ◽  
pp. 973-981
Author(s):  
Kevin C Keith ◽  
Molly Fitzgerald-Hayes

Abstract Each Saccharomyces cerevisiae chromosome contains a single centromere composed of three conserved DNA elements, CDE I, II, and III. The histone H3 variant, Cse4p, is an essential component of the S. cerevisiae centromere and is thought to replace H3 in specialized nucleosomes at the yeast centromere. To investigate the genetic interactions between Cse4p and centromere DNA, we measured the chromosome loss rates exhibited by cse4 cen3 double-mutant cells that express mutant Cse4 proteins and carry chromosomes containing mutant centromere DNA (cen3). When compared to loss rates for cells carrying the same cen3 DNA mutants but expressing wild-type Cse4p, we found that mutations throughout the Cse4p histone-fold domain caused surprisingly large increases in the loss of chromosomes carrying CDE I or CDE II mutant centromeres, but had no effect on chromosomes with CDE III mutant centromeres. Our genetic evidence is consistent with direct interactions between Cse4p and the CDE I-CDE II region of the centromere DNA. On the basis of these and other results from genetic, biochemical, and structural studies, we propose a model that best describes the path of the centromere DNA around a specialized Cse4p-nucleosome.


2020 ◽  
Vol 48 (6) ◽  
pp. 2769-2778
Author(s):  
Huilin Li ◽  
Nina Y. Yao ◽  
Michael E. O'Donnell

The replication of DNA in chromosomes is initiated at sequences called origins at which two replisome machines are assembled at replication forks that move in opposite directions. Interestingly, in vivo studies observe that the two replication forks remain fastened together, often referred to as a replication factory. Replication factories containing two replisomes are well documented in cellular studies of bacteria (Escherichia coli and Bacillus subtilis) and the eukaryote, Saccharomyces cerevisiae. This basic twin replisome factory architecture may also be preserved in higher eukaryotes. Despite many years of documenting the existence of replication factories, the molecular details of how the two replisome machines are tethered together has been completely unknown in any organism. Recent structural studies shed new light on the architecture of a eukaryote replisome factory, which brings with it a new twist on how a replication factory may function.


Biochemistry ◽  
2008 ◽  
Vol 47 (19) ◽  
pp. 5417-5423 ◽  
Author(s):  
Ashwani Kumar Vashishtha ◽  
Ann H. West ◽  
Paul F. Cook

1997 ◽  
Vol 25 (1) ◽  
pp. 78S-78S ◽  
Author(s):  
NATALIE M. SENIOR ◽  
GUILIANO SILIGARDI ◽  
ALEXANDER DRAKE ◽  
PAUL G. THOMAS ◽  
MARTIN J. WARREN

1998 ◽  
Vol 284 (5) ◽  
pp. 1565-1580 ◽  
Author(s):  
Vesa Tuominen ◽  
Pirkko Heikinheimo ◽  
Tommi Kajander ◽  
Tuire Torkkel ◽  
Teppo Hyytiä ◽  
...  

Biochemistry ◽  
2012 ◽  
Vol 51 (4) ◽  
pp. 857-866 ◽  
Author(s):  
Vidya Prasanna Kumar ◽  
Leonard M. Thomas ◽  
Kostyantyn D. Bobyk ◽  
Babak Andi ◽  
Paul F. Cook ◽  
...  

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