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Saccharomyces cerevisiae assembly

Fig. 2.3 The development of polarity and asymmetric division in Saccharomyces cerevisiae. The diagram is reproduced in a slightly simplified form from the work of Lew Reed (1995) with the permission of Current Opinion in Genetics and Development, (a) The F-actin cytoskeleton strands = actin cables ( ) cortical actin patches, (b) The polarity of growth is indicated by the direction of the arrows (arrows in many directions signifies isotropic growth), (c) 10-nm filaments which are assembled to form a ring at the neck between mother and bud. (d) Construction of the cap at the pre-bud site. Notice that the proteins of the cap become dispersed at the apical/isotropic switch, first over the whole surface of the bud, then more widely. Finally, secretion becomes refocussed at the neck in time for cytokinesis, (e) The status and distribution of the nucleus and microtubules of the spindle. Notice how the spindle pole body ( ) plays an important part in orientation of the mitotic spindle. Fig. 2.3 The development of polarity and asymmetric division in Saccharomyces cerevisiae. The diagram is reproduced in a slightly simplified form from the work of Lew Reed (1995) with the permission of Current Opinion in Genetics and Development, (a) The F-actin cytoskeleton strands = actin cables ( ) cortical actin patches, (b) The polarity of growth is indicated by the direction of the arrows (arrows in many directions signifies isotropic growth), (c) 10-nm filaments which are assembled to form a ring at the neck between mother and bud. (d) Construction of the cap at the pre-bud site. Notice that the proteins of the cap become dispersed at the apical/isotropic switch, first over the whole surface of the bud, then more widely. Finally, secretion becomes refocussed at the neck in time for cytokinesis, (e) The status and distribution of the nucleus and microtubules of the spindle. Notice how the spindle pole body ( ) plays an important part in orientation of the mitotic spindle.
Santamaria, P. G., Finley, D., Ballesta, j. P., and Remacha, M. Rpn6p, a proteasome subunit from Saccharomyces cerevisiae, is essential for the assembly and activity of the 26S proteasome. J Biol Chem 2003,... [Pg.245]

Figure 5.2. Organization of m/-specific and general Fe-S cluster assembly (isc) genes in A. vinelandii. The genes encoding for equivalent proteins or domains in Saccharomyces cerevisiae are shown for comparison. Figure 5.2. Organization of m/-specific and general Fe-S cluster assembly (isc) genes in A. vinelandii. The genes encoding for equivalent proteins or domains in Saccharomyces cerevisiae are shown for comparison.
Garland SA, Hoff K, Vickery LE, Culotta VC. 1999. Saccharomyces cerevisiae ISUl and ISU2 members of a well-conserved gene family for iron-snlfnr clnster assembly. J Mol Biol 294 897-907. [Pg.63]

Strain J, Lorenz CR, Bode J, et al. 1998. Supressors of superoxide dismutase (SODl) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly. J Biol Chem 273 31138-44. [Pg.65]

Pauli, T.T. and Johnson, R.C. (1995) DNA looping by Saccharomyces cerevisiae high mobility group proteins NHP6A/B. Consequences for nucleoprotein complex assembly and chromatin condensation. J. Biol. Chem. 270, 8744-8754. [Pg.128]

Arnason, T., and M. J. Ellison. Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol Cell Biol. 14 7876-83.1994. [Pg.125]

Frataxin is another protein which was shown to be targeted into hydrogenosomes (Dolezal et al. 2007). Importantly, I vaginalis frataxin can, in part, functionally replace mitochondrial frataxin, as demonstrated by its ability to partially restore defects in FeS cluster assembly in Saccharomyces cerevisiae Ayfhl mutants and frataxin-deficient Trypanosoma brucei (our unpublished data). In yeast, I vaginalis frataxin also partially restored defects in heme synthesis, although neither heme-containing proteins nor components involved in heme synthesis have been identified in T. vaginalis (Dolezal et al. 2007). [Pg.133]

Table 1 Components of FeS cluster assembly in Saccharomyces cerevisiae, Escherichia coli, and amitochondriate eukaryotes + high sequence similarity limited sequence similarity no similarity found. mtHSP70 (Ssql) proteins cannot be distinguished from other mtHSP70 isoforms (reanalyzed after Lill and Miihlenhoff 2005) ... Table 1 Components of FeS cluster assembly in Saccharomyces cerevisiae, Escherichia coli, and amitochondriate eukaryotes + high sequence similarity limited sequence similarity no similarity found. mtHSP70 (Ssql) proteins cannot be distinguished from other mtHSP70 isoforms (reanalyzed after Lill and Miihlenhoff 2005) ...
Rouault , Tong WH (2005) Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat Rev Mol Cell Biol 6 345-351 Roy A, Solodovnikova N, Nicholson T, Antholine W, Walden WE (2003) A novel eukaryotic factor for cytosolic Fe-S cluster assembly. EMBO J 22 4826-4835 Schilke B, Voisine C, Beinert H, Craig E (1999) Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae. Proc Natl Acad Sci USA 96 10206-10211... [Pg.229]

Iron-Sulfur Cluster Assembly in Saccharomyces cerevisiae... [Pg.116]

Coxl7, an 8.1-kDa cysteine-rich protein, was the first copper chaperone to be identified. Saccharomyces cerevisiae harboring mutations in coxl 7 are respiratory deficient, a phenotype resulting from their inability to assemble a functional cytochrome c oxidase complex (Glerum et al., 1996a). coxl7 mutant yeast are, however, able to express all the subunits of the cytochrome c oxidase complex, indicating that the lesion must lie in a posttranslational step that is essential for assembly of the functional complex in the mitochondrial membrane. Unlike other cytochrome c... [Pg.204]

Graham, L. A., Brandt, U., Sargent, J. S., and Trumpower, B. L., 1992, Mutational analysis of assembly and function of the iron-suUur protein of the cytochrome fcc, complex in saccharomyces cerevisiae, J. Bioenerg. Biomembr. 25 245n257. [Pg.576]

Macino G. and Tzagoloff A. (1979). Assembly of the mitochondrial membrane system partial sequence of a mitochondrial ATPase gene in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 76 131-135. [Pg.417]

Elgersma, Y., Van Den Berg, M., Tabak, H.F. Distel, B. (1993) Genetics ISSi, 731-740. An efficient positive selection procedure for the isolation of peroxisomal import and peroxisome assembly mutants of Saccharomyces cerevisiae. [Pg.375]

Y. -X. et al. (2012) Self-surface assembly of cellulosomes with two miniscaffoldins on Saccharomyces cerevisiae for cellu-losic ethanol production. Proc. Natl Acad. Sci. US.A., 109, 13260-13265. [Pg.683]

What follows is largely based on the known sequence of events during wall assembly in Saccharomyces cerevisiae. Details of it may not be universally applicable. [Pg.171]


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