ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Expression of Genes on Human Chromosome 21 (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 450 (1985), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1985.tb21482.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Evidence that mammalian glutamine-dependent carbamyl phosphate synthetase arose through gene fusion (1992)
    Springer
    Journal of molecular evolution 35 (1992), S. 217-222 
    Details
    ISSN: 1432-1432
    Keywords: Mammalian glutamine-dependent carbamyl phosphate synthetase ; Gene fusion ; CAD gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary On the basis of homology, the mammalian CAD (glutamine-dependent carbamyl phosphate synthetase-aspartate transcarbamylase-dihydroorotase) gene appears to have arisen from the fusion of four separate ancestral genes. Evidence for two of these precursor genes is found in the carbamyl phosphate synthetase (CPSase) domain of CAD. In prokaryotes, such as Escherichia coli CPSase is encoded by two distinct cistrons of the carAB operon. Whereas carA and carB are separated by a short noncoding intercistronic region, the homologous sequences of the CAD gene encode an amino acid bridge. This bridge connects the subdomains of the CAD CPSase. We constructed a bacterial carAB fusion gene in which the intercistronic region codes for a hamster bridgelike sequence. The fused carAB gene directs the synthesis of a stable bifunctional polypeptide whose glutamine-dependent CPSase activity is comparable to the E. coli CPSase holoenzyme. The fusion in E. coli of the single gene counterparts of CAD demonstrates a potential model system to study the genetic events that lead to gene fusion and the creation of multienzymatic proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00178597
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Mapping of the gene encoding the multifunctional protein carrying out the first three steps of pyrimidine biosynthesis to human chromosome 2 (1989)
    Springer
    Human genetics 〈Berlin〉 82 (1989), S. 40-44 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The CAD gene encodes a trifunctional protein that carries the activities of the first three enzymes (carbamyl phosphate synthetase II, aspartate transcarbamylase, and dihydroorotase) of de novo pyrimidine biosynthesis. Genomic fragments of the human CAD gene have been obtained by screening a human genomic library in bacteriophage lambda using a Syrian hamster cDNA clone as a probe. These human genomic clones have been used to assign the CAD gene to human chromosome 2 using in situ hybridization to human metaphase chromosomes and Southern blot hybridization analysis of DNA isolated from a panel of Chinese hamster/human hybrid cells. In situ hybridization analysis has allowed further localization of this gene to the chromosomal region 2p21-p22.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00288269
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    An altered chloroplast ribosomal protein in ery-M1 mutants of Chlamydomonas reinhardi (1974)
    Springer
    Molecular genetics and genomics 132 (1974), S. 119-129 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A unified biochemical and genetic study has led to the location of the gene for erythromycin resistance in 4 mutants of Chalamydomonas reinhardi and the identification of the chloroplast ribosomal protein altered in these strains. Tetrad analyses of crosses involving the Mendelian mutants ery-M1a, ery-M1b, ery-M1c, and ery-M1d indicate that they are closely-linked alleles which map to nuclear linkage group XI. The proteins of the 52s subunits of wild-type and the 4 ery-M1 mutants were compared by one-and two-dimensional gel electrophoresis. Protein LC6 from wild-type differs in net charge at pH 5 from the homologous component found in each of the mutants. The LC6 in ery-M1b is also 30% smaller in molecular weight than the wild-type protein. The variety of altered forms of LC6 observed and the allelic nature of the genetic determinants strongly support the view that the nuclear locus for erythromycin resistance of the ery-M1 group is the structural gene for the chloroplast ribosomal protein LC6.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00272177
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Characterization of chloroplast and cytoplasmic ribosomal proteins of Chlamydomonas reinhardi by two-dimensional gel electrophoresis (1974)
    Springer
    Molecular genetics and genomics 132 (1974), S. 105-118 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Proteins from chloroplast and cytoplasmic ribosomes of Chlamydomonas reinhardi were mapped by a two-dimensional gel electrophoresis system which also permitted their molecular weights to be determined. Estimates of the numbers of proteins in the ribosomal subunits are: small chloroplast, 22; small cytoplasmic, 26; large chloroplast, 26; large cytoplasmic, 39. Two pairs of proteins of the small subunits and four pairs of the large subunits had similar electrophoretic mobilities in both dimensions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00272176
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Suppression of erythromycin resistance in ery-M1 mutants of Chlamydomonas reinhardi (1977)
    Springer
    Molecular genetics and genomics 157 (1977), S. 39-46 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary After mutagenesis of the erythromycin-resistant Chlamydomonas reinhardi strain ery-M1b, four mutants were isolated, each more sensitive to erythromycin than ery-M1b. All four mutants carry the original ery-M1b mutation which confers resistance and a separate mutation (es) which partially suppresses resistance. The mutants are designated es5ery-M1b, es101ery-M1b, es105ery-M1b, and es115ery-M1b. The suppressor mutations represent at least three different Mendelian loci. The suppressor es101 is located on the same linkage group as ery-M1, while the other suppressors are not linked to ery-M1. Although some of these suppressors can also mask the erythromycin resistance of ery-M2 strains, none had any effect on the non-Mendelian mutant ery-Ula. In addition, each suppressor affected the cross-resistance of ery-M1 mutants to other antibiotics. At least two of the changes in cross-resistance are due solely to the suppressor. Chloroplast ribosomes from cells carrying es5ery-M1b, es101ery-M1b, and es115ery-M1b have a greater affinity for 14C-erythromycin in vitro than those from ery-M1b. The degree of affinity depends upon the concentration of KCl. Each of these Mendelian suppressors probably affects a chloroplast ribosome function. Hence, a number of nuclear genes must play roles in the biogenesis of the chloroplast ribosome in Chlamydomonas reinhardi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268685
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    The aspartate transcarbamylase domain of a mammalian multifunctional protein expressed as an independent enzyme in Escherichia coli (1988)
    Springer
    Molecular genetics and genomics 213 (1988), S. 278-284 
    Details
    ISSN: 1617-4623
    Keywords: Pyrimidine biosynthesis ; Multifunctional proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Although aspartate transcarbamylase (ATCase) is an independent, monofunctional enzyme in Escherichia coli, mammalian ATCase is one of the globular enzymatic domains of the multifunctional CAD protein. We subcloned fragments of the hamster CAD cDNA and assayed polypeptide products expressed in E. coli for ATCase activity in order to isolate a stretch of cDNA which encodes only the ATCase domain. Three such expression constructs contain fragments of hamster CAD cDNA similar in length to the gene encoding the E. coli ATCase catalytic subunit (pyrB). These constructs yield stable proteins with ATCase activity, ascertained by both in vivo and in vitro assays; the clones also possess sequence homology with the pyrB gene at both the 5′ and 3′ ends. The clone producing the most active ATCase contains cDNA which is analogous to the entire pyrB gene, plus a small amount of CAD sequence upstream of this region. Because these constructs produce independently folded, active ATCase from a piece of cDNA the size of the E. coli pyrB gene, they open the door for the in-depth investigation of the isolated mammalian enzyme domain utilizing recombinant DNA technology. This approach is potentially useful for the analysis of domains of other multifunctional proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00339592
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Complete hamster CAD protein and the carbamylphosphate synthetase domain of CAD complement mammalian cell mutants defective in de novo pyrimidine biosynthesis (1992)
    Springer
    Somatic cell and molecular genetics 18 (1992), S. 309-318 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The mammalianCAD gene codes for a 240-kDa multifunctional protein that catalyzes the first three steps of de novo pyrimidine biosynthesis. Previously, the longest cDNA construct available was missing approximately 500 bp of coding sequence at the 5′ end, thereby lacking the sequence to encode the entire carbamylphosphate synthetase (CPSase) domain. Here, a completeCAD hamster cDNA is constructed, placed into a mammalian expression vector, and transfected into hamster cells deficient in CAD. Transfectants show coordinately restored levels of all three enzyme activities and the presence of full-length CAD protein. A derivative construct of theCAD cDNA was generated that should encode only the CPSase domain. When transfected into mammalian cells, a protein was synthesized that had significant CPSase activity both in vivo and in vitro. The two constructs generated in this study will facilitate the study of CAD structure, function, and allosteric regulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01235754
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Biochemical genetic analysis of pyrimidine biosynthesis in mammalian cells: III. Association of carbamyl phosphate synthetase, aspartate transcarbamylase, and dihydroorotase in mutants of cultured Chinese hamster cells (1979)
    Springer
    Somatic cell and molecular genetics 5 (1979), S. 175-191 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Carbamyl phosphate synthetase (EC 2.7.2.9), aspartate transcarbamylase (EC 2.1.3.2), and dihydroorotase (EC 3.5.2.3), the first three enzymes in de novo pyrimidine synthesis in Chinese hamster ovary cell strain Kl (CHO-Kl), cosediment through a glycerol gradient. When an extract from Urd− A, a pyrimidine-requiring auxotroph reduced in all three activities, is run on a glycerol gradient, the enzyme activities appear in two peaks higher in the gradient, a peak of aspartate transcarbamylase separated from a peak of carbamyl phosphate synthetase and dihydroorotase. Revertants of Urd− A have increased activity of all three enzymes and give glycerol gradient patterns similar to either CHO- Kl or Urd− A. The gradient pattern for Urd− A and some of its revertants can be mimicked by treating the CHO- Kl cell extract with trypsin. Hybrids made between a CHO-Kl purine- requiring auxotroph (Ade− C) and a Urd− A revertant gave a glycerol gradient pattern which is a composite of the CHO- Kl and revertant patterns. A model is presented for the structure of this multifunctional protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01539159
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Identification and localization of DNA alteration in Chinese hamster ovary cell mutants (Urd−) defective in the first three enzymes of de novo pyrimidine synthesis (1985)
    Springer
    Somatic cell and molecular genetics 11 (1985), S. 379-390 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract In animals, the first three enzymatic steps of de novo pyrimidine synthesis, carbamyl phosphate synthetase, aspartate transcarbamylase, and dihydroorotase, comprise the multifunctional protein known as the CAD protein. Mutants of Chinese hamster ovary cells (CHO-K1, pro−) deficient in CAD protein activities require uridine for growth and are designated Urd− A mutants. To examine further the nature of the genetic alterations in Urd− A mutants and revertants, we have performed a detailed Southern blot hybridization analysis of DNA from wild-type, Urd− A, and revertant cells using as hybridization probes cDNAs complementary to CAD mRNA isolated from Syrian hamster. This has allowed us to identify an apparent alteration in the CAD gene in DNA from Urd− A cells. This alteration is in a region of the gene which appears to correspond to the region of the protein which is hypersensitive to proteases and which seems to be altered in the mutants. Only one of the two CAD alleles present appears to be altered in this way. Study of certain revertants of Urd− A strongly suggests that in some cases reversion has occurred by amplification of the mutant CAD allele.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01534415
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...