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  • 1
    Electronic Resource
    Electronic Resource
    Sequence analysis of a 10 kb DNA fragment from yeast chromosome VII reveals a novel member of the dnaJ family (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 145-148 
    Details
    ISSN: 0749-503X
    Keywords: genome sequencing ; Saccharomyces cerevisiae ; chromosome VII ; CEG1 ; SOH1 ; DnaJ ; SCS3 ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the sequence analysis of a 10 kb DNA fragment of Saccharomyces cerevisiae chromosome VII. This sequence contains four complete open reading frames (ORFs) of greater than 100 amino acids. There are also two incomplete ORFs flanking the extremes: one of these, G2868, is the 5′ part of the SCS3 gene (Hosaka et al., 1994). ORFs G2853 and G2856 correspond to the genes CEG1, coding for the alfa subunit of the mRNA guanylyl transferase and a 3′ gene of unknown function previously sequenced (Shibagaki et al., 1992). G2864 is identical to SOH1 also reported (Fan and Klein, 1994). The translated sequence of G2861 is similar to the human dnaJ homolog. The nucleotide sequence reported here has been entered in the EMBL Data Library under the Accession Number X87252.
    Additional Material: 4 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    Invertase secretion in Hansenula polymorpha under the AOX1 promoter from Pichia pastoris (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 815-822 
    Details
    ISSN: 0749-503X
    Keywords: HARS, Hansenula autonomously replicating sequence ; SUC2, sucrose invertase ; AOX1, alcohol oxidase ; Pollk, polymerase I, fragment klenow ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A DNA fragment containing a transcription regulating region of the alcohol oxidase (AOX1) gene from the methylotrophic yeast Pichia pastoris was used in the construction of a vector for the expression of heterologous proteins in the methylotrophic yeast Hansenula polymorpha. We used this vector to clone the SUC2 gene from Saccharomyces cerevisiae into H. polymorpha yeast.The culture conditions for invertase production using a fed-batch culture were studied. More than 1·5×103 U/ml of biologically active invertase (1 g/l) were secreted to the cellular periplasmic space. The fermentative process was scaled up to 50 l.Invertase produced from H. polymorpha was glycosylated, but it contained significantly less carbohydrate than protein produced by S. cerevisiae. Using the Western-blot technique, it was observed that invertase secreted from H. polymorpha and invertase secreted from S. cerevisiae showed common antigenic determinants.
    Additional Material: 5 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of a putative methylenetetrahydrofolate reductase by sequence analysis of a 6·8 kb DNA fragment of yeast chromosome VII (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1047-1051 
    Details
    ISSN: 0749-503X
    Keywords: genome sequencing ; Saccharomyces cerevisiae ; chromosome VII ; methylenetetrahydrofolate reductase ; SCS3 ; SUP44 ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the sequence analysis of a 6·8 kb DNA fragment from Saccharomyces cerevisiae chromosome VII. This sequence contains five open reading frames (ORFs) greater than 100 amino acids. There is also an incomplete ORF flanking one of the extremes, G2868, which is the 3′ end of the SCS3 gene (Hosaka et al., 1994). The translated sequence of ORF G2882 shows similarity to the human methylenetetrahydrofolate reductase (Goyette et al., 1994). ORF G2889 shows no significant homologies with the sequences compiled in databases. ORF G2893 corresponds to the gene SUP44, coding for the yeast ribosomal protein S4 (All-Robin et al., 1990). G2873 and G2896 are internal ORFs. The whole sequence of the fragment is available at the EMBL nucleotide sequence database, GenBank and Data Bank of Japan under the Accession Number X94106.
    Additional Material: 2 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of the ribosomal binding site in rat liver rough microsomes: Ribophorins I and II, two integral membrane proteins related to ribosome binding (1978)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 8 (1978), S. 279-302 
    Details
    ISSN: 0091-7419
    Keywords: rat liver endoplasmic reticulum ; rough microsomes ; membrane-bound polysomes ; ribosome-binding sites ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Rat liver rough endoplasmic reticulum membranes (ER) contain two characteristic transmembrane glycoproteins which have been designated ribophorins I and II and are absent from smooth ER membranes. These proteins (MW 65,000 and 63,000 respectively) are related to the binding sites for ribosomes, as suggested by the following findings: (i) The ribophorin content of the rough ER membranes corresponds stoichiometrically to the number of bound ribosomes; (ii) ribophorins are quantitatively recovered with the bound polysomes after most other ER membrane proteins are dissolved with the nonionic detegent Kyro EOB; (iii) in intact rough microsomes ribophorins can be crosslinked chemically to the ribosomes and therefore are in close proximity to them.Treatment of rough microsomes with a low Triton X-100 concentration leads to the lateral displacement of ribosomes on the microsomal surface and to the formation of aggregates of bound ribosomes in areas of membranes which frequently invaginate into the microsomal lumen. Subfractionation of Triton-treated microsomes containing invaginations led to the recovery of smooth and “rough-inverted” vesicles. Ribophorins were present only in the latter fraction, indicating that both proteins are displaced together with the ribosome-binding capacity of rough and smooth microsomal membranes reconstituted after solubilization with detergents sugest that ribophorins are necessary for in vitro ribosome binding. Ribophorin-like proteins were found in rough microsomes obtained from secretory tissues of several animal species. The two proteins present in rat lacrimal gland microsomes have the same mobility as hepatocyte ribophorins and cross-react with antisera against them.
    Additional Material: 18 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400080307
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  • 5
    Electronic Resource
    Electronic Resource
    Functional conservation of cytosolic proteins required for endosomal vesicle fusion (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1251-1262 
    Details
    ISSN: 0749-503X
    Keywords: yeast ; Sec18 ; endocytosis ; NEM ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Recent studies suggest that intracellular membrane traffic relies upon families of related proteins which confer specificity to individual transport reactions but which operate in tandem with a ubiquitous fusogenic complex containing the N-ethylmaleimide-sensitive fusion protein (NSF). The extent to which components of this process are functionally conserved is apparent from the finding that yeast Sec18 protein (Sec18p) can substitute for mammalian NSF in intra-Golgi transport reactions. Here we report that yeast cytosol can support mammalian endosomal vesicle fusion, demonstrating conservation of cytosolic components required for this reaction. Furthermore, under conditions in which the fusion reaction is NSF-dependent we show that yeast Sec18p can functionally substitute for NSF, showing that the yeast protein is capable of catalysing at least two distinct mammalian membrane fusion events. In addition we exploit the complex pattern of sensitivity of the mammalian reaction to N-ethylmaleimide (NEM), coupled with the use of yeast cytosol, to dissect a number of factors required for fusion. We reveal at least three novel NEM-sensitive activities. One of these can be restored by yeast cytosol suggesting that it is functionally conserved.
    Additional Material: 6 Ill.
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  • 6
    Electronic Resource
    Electronic Resource
    Cloning of the Penicillium minioluteum gene encoding dextranase and its expression in Pichia pastoris (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1187-1200 
    Details
    ISSN: 0749-503X
    Keywords: dextranase ; Penicillium minioluteum ; Pichia pastoris ; heterologous gene expression ; protein secretion ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The DEX gene encoding an extracellular dextranase was isolated from the genomic DNA library of Penicillium minioluteum by hybridization using the dextranase cDNA as a probe. Comparison of the gene and cDNA sequences revealed that the DEX gene does not contain introns. Amino acid sequences comparison of P. minioluteum dextranase with other reported dextranases reveals a significant homology (29% identity) with a dextranase from Arthrobacter sp. CB-8. The DEX gene fragment encoding a mature protein of 574 amino acids was expressed in the methylotrophic yeast Pichia pastoris by using the SUC2 gene signal sequence from Saccharomyces cerevisiae under control of the alcohol oxidase-1 (AOX1) promoter. Over 3·2g/l of enzymatically active dextranase was secreted into the medium after induction by methanol. The yeast product was indistinguishable from the native enzyme in specific activity and the N-terminus of both proteins were identical.
    Additional Material: 8 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    CtCdc55p and CtHal3p: Two putative regulatory proteins from Candida tropicalis with long acidic domains (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1321-1329 
    Details
    ISSN: 0749-503X
    Keywords: Candida tropicalis ; CDC55 ; HAL3 ; protein phosphatase ; acidic domain ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The salt-tolerance gene HAL3 from Saccharomyces cerevisiae encodes a novel regulatory protein (Hal3p) which modulates the expression of the ENA1 sodium-extrusion ATPase (Ferrando et al., Mol. Cell. Biol. vol.15, 1995, pp.5470-5481). Hal3p contains an essential acidic domain rich in aspartates at its carboxyl terminus. We have isolated two cross-hybridizing genes from a genomic library of Candida tropicalis. One of the genes (CtHAL3) is a true homolog of HAL3 and it partially complements the salt sensitivity of a S. cerevisiae hal3 mutant. The activity of CtHAL3 was equivalent to that of an open reading frame (YKL088w) identified by genome sequencing of S. cerevisiae and with homology to HAL3. The other cross-hybridizing gene (CtCDC55) is a CDC55 homolog, encoding a protein with an internal acidic domain not present in the S. cerevisiae CDC55 product. Cdc55p is a regulatory subunit of protein phosphatase 2A and CtCDC55 complements the cold sensitivity of a S. cerevisiae cdc55 mutant. The presence of acidic domains in different putative regulatory proteins may suggest a role for this type of domain in molecular interactions. Sequences have been deposited in the EMBL data library under Accession Numbers X88899 (CtCDC55) and X88900 (CtHAL3).
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