Library

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
Filter
  • Calcineurin A  (1)
  • Mating-less mutants  (1)
  • Microtubule  (1)
  • 1
    Electronic Resource
    Electronic Resource
    An electron microscopic study on the mating tube formation in the heterobasidiomycete Tremella mesenterica (1980)
    Springer
    Archives of microbiology 128 (1980), S. 215-221 
    Details
    ISSN: 1432-072X
    Keywords: Mating tube ; Microtubule ; Tremella ; Ultrastructure ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Ultrastructure of the mating tube formed in yeast haplont of the heterobasidiomycete Tremella mesenterica was studied by electron microscopy. Cell wall of the mating tube emerged as evagination of the inner layers, rupturing outer layers of the mother cell wall. Comparison with budding cells suggested that the tube emergence place at bud scar and the process of tube emergence was the same as that of bud emergence. Electron transparent vesicles of 0.1 μm diameter were scattered in the cytoplasm of the mating tube. Nucleus-associated organelle was located at one side of the nuclear envelope which extended towards the mating tube. A few microtubules were detected in the mating tube, but their association with a nucleus was not clear. The cytoplasmic structure of the mating tube was discussed in comparison with that of hyphae of the filamentous fungi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00406161
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Topographic and quantitative changes in cell-surface acid-phosphatase during the sexual differentiation of the heterobasidiomycete, Tremella mesenterica (1984)
    Springer
    Archives of microbiology 139 (1984), S. 184-187 
    Details
    ISSN: 1432-072X
    Keywords: Tremella mesenterica ; Sexual differentiation ; Acid phosphatase ; Histochemical staining ; Mating-less mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract During the hormonal induction of the sexual differentiation in the heterobasidiomycetous yeast, Tremella mesenterica, mating type ab cells, the notable increase in acid phosphatase (ACPase) activity was found in cell surface. Electron-microscopic observation by activity straining revealed that the increase in ACPase was specifically occurred at the surface of mating tubes of differentiated cells. The increase in ACPase on cell surface was not induced in all three-types of mating-less mutant strains. Gl-arrest-negative, mating-tube-defective and conjugation-defective strains of ab cells. Thus, it might be concluded that the characteristic arrangement of ACPase caused by sexual differentiation plays a physiological role for cell-cell recognition and/or cell-cell fusion as early events in alteration of generation from vegetative propagation to sexual one.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00401997
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    TheSaccharomyces cerevisiae genes (CMP1 andCMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B (1991)
    Springer
    Molecular genetics and genomics 227 (1991), S. 52-59 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Calmodulin-binding protein ; Protein phosphatase (2B type) ; Calcineurin A
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Saccharomyces cerevisiae genomic clones that encode calmodulin-binding proteins were isolated by screening a λgt11 expression library using125I-labeled calmodulin as probe. Among the cloned yeast genes, we found two closely related genes (CMP1 andCMP2) that encode proteins homologous to the catalytic subunit of phosphoprotein phosphatase. The presumed CMP1 protein (62999 Da) and CMP2 protein (68496 Da) contain a 23 amino acid sequence very similar to those identified as calmodulin-binding sites in many calmodulin-regulated proteins. The yeast genes encode proteins especially homologous to the catalytic subunit of mammalian phosphoprotein phosphatase type 213 (calcineurin). The products of theCMP1 andCMP2 genes were identified by immunoblot analysis of cell extracts as proteins of 62000 and 64000 Da, respectively. Gene disruption experiments demonstrated that elimination of either or both of these genes had no effect on cell viability, indicating that these genes are not essential for normal cell growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00260706
    Library Location Call Number Volume/Issue/Year 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...