GLORIA

GEOMAR Library Ocean Research Information Access

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
    Detecting human bacterial contamination in Antarctic soils (2000)
    Springer
    Polar biology 23 (2000), S. 644-650 
    Details
    ISSN: 1432-2056
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The presence of non-indigenous microbial contaminants resulting from human faecal contamination of old and currently occupied base and field camp sites in South Victoria Land, Antarctica, was assessed by PCR amplification of extracted soil DNA using species-specific PCR primers. Positive controls (samples recovered from the environs of Scott Base, including the sewage outfall) gave strong signals with Escherichia coli primers whereas Clostridium clostridiiforme primers yielded a signal only with the sewage outfall sample. A comparison was made of PCR amplification results from samples from the abandoned Canada Glacier camp site, the Lake Fryxell summer camp site, the Cape Bird Adelie penguin colony and pristine sites from relatively inaccessible regions of the Taylor Valley. Results indicated a possible residual level of E. coli contamination in the abandoned Canada Glacier camp site, but no significant contamination of the currently occupied Lake Fryxell camp site. These data may provide indirect evidence for improved awareness and standards of waste handling and disposal over the past two decades of Dry Valley field research.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003000000137
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Tissue-specific differences of the mitochondrial protein import machinery: in vitro import, processing and degradation of the pre-F1β subunit of the ATP synthase in spinach leaf and root mitochondria (1994)
    Springer
    Plant molecular biology 26 (1994), S. 571-579 
    Details
    ISSN: 1573-5028
    Keywords: plant mitochondria ; protein degradation ; protein import ; protein processing ; spinach roots ; tissue-dependency
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In this study we report the first comparison of the mitochondrial protein import and processing events in two different tissues from the same organism. Both spinach leaf and root mitochondria were able to import and process the in vitro transcribed and translated Neurospora crassa F1β subunit of ATP synthase to the mature size product. Temperature optimum for protein import, 20 °C, was considerably lower than that found in other systems. In spinach leaf mitochondria, the processing peptidase has been shown to constitute an integral part of the bc1 complex of the respiratory chain. In accordance with these results, the majority of the processing activity in root mitochondria was also localized in the membrane. However, although the same amount of the processing peptidase was present per mg of membrane protein in both leaf and root mitochondria, as determined immunologically, the specific processing activity was several-fold higher in roots. Furthermore, in contrast to the processing enzyme in leaf, a portion of the processing activity could be disassociated from the root membrane with relatively weak salt treatment. The processing event in both the leaf and root membranes was always accompanied by a degradation of the F1β precursor. The degradation activity was found to be several-fold higher in roots than in leaves and was also partially dissociated from the membrane after salt treatment. Both the processing and degradation activities were inhibited by orthophenanthroline, a known metalloprotease inhibitor. These results show tissue-specific differencies of the processing event catalyzed by the bc1 complex and indicate the presence of two populations of the processing peptidase in root mitochondria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00013744
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Characterization of the bifunctional mitochondrial processing peptidase (MPP)/bc 1 complex inSpinacia oleracea (1996)
    Springer
    Journal of bioenergetics and biomembranes 28 (1996), S. 285-292 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondrial processing peptidase MPP ; bc 1 complex ; protein import ; plant mitochondria ; cytochromec reductase ; protein processing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The mitochondrial general processing peptidase (MPP) in plant mitochondria constitutes an integral part of the cytochromebc 1 complex of the respiratory chain. Here we present a characterization of this bifunctional complex from spinach leaf mitochondria. The purified MPP/bc 1 complex has a molecular mass of 550 kDa, which corresponds to a dimer. Increased ionic strength results in partial dissociation of the dimer as well as loss of the processing activity. Micellar concentrations of nonionic and zwitterionic detergents stimulate the activity by decreasing the temperature optimum of the processing reaction, whereas anionic detergents totally suppress the activity. MPP is a metalloendopeptidase. Interestingly, hemin, a potent regulator of mitochondrial and cytosolic biogenesis and inhibitor of proteosomal degradation, inhibits the processing activity. Measurements of the processing activity at different redox states of thebc 1 complex show that despite bifunctionality of the MPP/bc 1 complex, there is no correlation between electron transfer and protein processing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02110702
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Mitochondrial protein import in plants – Signals, Sorting, Targeting, Processing and Regulation (1998)
    Springer
    Plant molecular biology 38 (1998), S. 311-338 
    Details
    ISSN: 1573-5028
    Keywords: mitochondrial processing peptidase ; molecular chaperones ; plant mitochondria ; protein import ; processing peptidase ; protein processing ; protein sorting ; regulation of protein import ; signal peptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mitochondrial biogenesis requires a coordinated expression of both the nuclear and the organellar genomes and specific intracellular protein trafficking, processing and assembly machinery. Most mitochondrial proteins are synthesised as precursor proteins containing an N-terminal extension which functions as a targeting signal, which is proteolytically cleaved off after import into mitochondria. We review our present knowledge on components and mechanisms involved in the mitochondrial protein import process in plants. This encompasses properties of targeting peptides, sorting of precursor proteins between mitochondria and chloroplasts, signal recognition, mechanism of translocation across the mitochondrial membranes and the role of cytosolic and organellar molecular chaperones in this process. The mitochondrial protein processing in plants is catalysed by the mitochondrial processing peptidase (MPP), which in contrast to other sources, is integrated into the bc1 complex of the respiratory chain. This is the most studied component of the plant import machinery characterised to date. What are the biochemical consequences of the integration of the MPP into an oligomeric protein complex and how are several hundred presequences of precursor proteins with no sequence similarities and no consensus for cleavage, specifically cleaved off by MPP? Finally we will address the emerging area of the control of protein import into mitochondria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006020208140
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Feature-extraction from endopeptidase cleavage sites in mitochondrial targeting peptides (1998)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 30 (1998), S. 49-60 
    Details
    ISSN: 0887-3585
    Keywords: kohonen network ; mitochondrial processing peptidase (MPP) ; mitochondrial intermediate peptidase (MIP) ; neural network ; protein import ; sequence motif ; mitochondrial targeting ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Cleavage sites in nuclear-encoded mitochondrial protein targeting peptides (mTPs) from mammals, yeast, and plants have been analysed for characteristic physicochemical features using statistical methods, perceptrons, multilayer neural networks, and self-organizing feature maps. Three different sequence motifs were found, revealing loosely defined arginine motifs with Arg in positions -10, -3, and -2. A self-organizing feature map was able to cluster these three types of endopeptidase target sites but did not identify any species-specific characteristics in mTPs. Neural networks were used to define local sequence features around precursor cleavage sites. Proteins 30:49-60, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...