Saccharomyces cerevisiae structure

Bousset, L., Belrhali, H., Janin,J., Melki, R., and Morera, S. (2001a). Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure 9, 39-46. 

R Sanchez, A Sail. Large-scale protein structure modeling of the Saccharomyces cerevisiae genome. Proc Natl Acad Sci USA 95 13597-13602, 1998. 

If a phylogenetic comparison is made of the 16S-Iike rRNAs from an archae-bacterium Halobacterium volcanii), a eubacterium E. coli), and a eukaryote (the yeast Saccharomyces cerevisiae), a striking similarity in secondary structure emerges (Figure 12.40). Remarkably, these secondary structures are similar despite the fact that the nucleotide sequences of these rRNAs themselves exhibit a low degree of similarity. Apparently, evolution is acting at the level of rRNA secondary structure, not rRNA nucleotide sequence. Similar conserved folding patterns are seen for the 23S-Iike and 5S-Iike rRNAs that reside in the... 

Five structural genes for amino acid uptake systems have been cloned in Saccharomyces cerevisiae by functional complementation, and their putative amino acid sequences deduced from the respective nucleotide sequences (Fig. 2). 

Despite the limited information available, rather clear predictions can be made about the probable structure, location, and energy coupling of the amino acid transporters of Saccharomyces cerevisiae, by comparing them with better known systems in both prokaryotes and eukaryotes. 

Yeast Insoluble Polysaccharide. The structure of an insoluble polysaccharide from the yeast Saccharomyces cerevisiae was investigated by Zechmeister and Toth,90a and also by Hassid, Joslyn and McCready.904 The isolation904 of 2,4,6-trimethyl-D-glucose as the sole product of the hydrolysis of the methylated polysaccharide indicated a chain of gluco-pyranose units joined by 1,3-glucosidic linkages. 

Bousset, L., Redeker, V., Decottignies, P., Dubois, S., Le Marechal, P., and Melki, R. (2004). Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p. Biochemistry 43, 5022-5032. 

Thual, C., Komar, A. A., Bousset, L., Fernandez-Bellot, E., Cullin, C., and Melki, R. (1999). Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2./. Biol. Chem. 274, 13666-13674. 

Hunte, C., Koepke, J., Lange, C., Rossmanith, T. and Michel, H. (2000) Structure at 2.3 A resolution of the cytochrome bcj complex from the yeast Saccharomyces cerevisiae with an antibody Fv fragment, Structure, 8, 669-684. 

E2 are structurally and functionally diverse. Early biochemical work by using reticulocyte system revealed five distinct proteins with properties of E2. With the advent of genome sequencing, this observation has been corroborated. Even simple eukaryotes like yeast Saccharomyces cerevisiae) have 13 genes potentially encoding E2s. The number of E2s in mammals is estimated to be in the range of 25-30. 

The structure of mannose-rich polysaccharide core in GL4 is close to that of yeast mannan (from Saccharomyces cerevisiae), which was inactive for IL-6 induction in a human peripheral whole-blood cells test system. This fact suggests that not the mannose moieties but other components, such as the lipophilic moiety and/or phosphates, are important for the activity. The lipophilic products in HF-hydrolysate of GL4 were then analyzed. In addition to peaks corresponding to the known fatty acids (C16 0, C18 1), two other unknown ion peaks at m/z 330 and 356 were found by FAB-MS (data not shown). 

More recently, workers in Japan published the solution structure of yeast (Saccharomyces cerevisiae) apo-calmodulin (PDB ILKJ). Yeast calmodulin is 60% identical in its amino acid sequence with vertebrate CaMs. The ILKJ N-terminal domain with its two helix-loop-helix calcium-binding domains looks quite similar to those of IDMO and ICFD (see Figure 6.23). 

Lowary, P.T. and Widom, J. (1989) Higher-order structure of Saccharomyces cerevisiae chromatin. Proc. Natl. Acad. Sci. USA 86, 8266-8270. 

Several lines of evidence indicate that CENP-A replaces conventional H3 in the nucleosome. Biochemical studies showed that CENP-A co-sediments with nucleo-some core particles [7] and a genetic analysis indicates an interaction between Cse4p, the CENP-A of Saccharomyces cerevisiae, and H4 [16,17]. A recent study with CENP-A purified from HeLa cells or expressed in bacteria showed that it can substitute for conventional H3 in nucleosome reconstitution [18]. Reconstituted CENP-A-containing nucleosomes appear to contain the other core histones in appropriate stoichiometry. However, they did not strongly protect 146 bp of core DNA from micrococcal nuclease, suggesting that CENP-A may significantly alter some aspects of the core nucleosome structure. 

Wu, L. and Winston, F. (1997) Evidence that Snf-Swi controls chromatin structure over both the TATA and UAS regions of the SUC2 promoter in Saccharomyces cerevisiae. Nucleic Acids Res. 25, 4230-4234. 

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