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  • 1
    Electronic Resource
    Electronic Resource
    The 26S-proteasome: regulation and substrate recognition (1997)
    Springer
    Molecular biology reports 24 (1997), S. 39-44 
    Details
    ISSN: 1573-4978
    Keywords: ATPase ; 26S proteasome ; programmed cell death ; regulators
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract There is extensive reprogramming of the ATPase regulators of the 26S proteasome before the programmed elimination of the abdominal intersegmental muscles (ISM) after eclosion in Manduca sexta [1]. This extensive ATPase reprogramming only occurs in ISM which are destined to die and not in flight muscle (FM). The MS73 ATPase also increases in the proleg retractor muscles which die at a developmentally different stage to ISM. The non-ATPase regulator S5a shows a similar increase to the ATPase regulators. We have cloned the Manduca SUG2 ATPase and shown that this ATPase is a component of the 26S proteasome. This ATPase shows a similar increase in concentration to the other ATPases in 26S proteasomes before muscle death. The SUG2 ATPase is also associated with other smaller complexes besides the 26S proteasome which act as activators of the 26S proteasome. Finally, in a yeast two-hybrid genetic screen we have identified a protein in human brain which interacts with the MS73 ATPase (and human S6). The interacting protein contains 6 ankyrin repeats and is co-immunoprecipitated with anti-MS73 antiserum after in vitro transcription/translation. The ankyrin repeat protein may interact with the MS73 ATPase as part of the substrate recognition process by the 26S proteasome. Many proteins degraded by the 26S proteasome contain ankyrin repeats, e.g. IkB and some cyclins: binding through ankyrin repeats to an ATPase regulator may complement protein ubiquitination and S5a binding as recognition signals by the 26S proteasome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006800522814
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Activator complexes containing the proteasomal regulatory ATPases S10b (SUG2) and S6′ (TBP1) in different tissues and organisms (1999)
    Springer
    Molecular biology reports 26 (1999), S. 35-38 
    Details
    ISSN: 1573-4978
    Keywords: activator complex ; ATPase ; 26S proteasome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Each 19S regulator of the 26S proteasome contains six ATPase subunits as well as many (〉14) non-ATPase protein subunits. The ATPase subunits have been detected in other complexes which may regulate transcription and possibly other cellular processes. The S10b (yeast SUG2 or human p42) and the S6′ (TBP1) ATPases have been found in an activator complex (modulator) prepared from bovine red cells. We have identified and partially characterised a similar activator from different human tissues (from soluble extracts of human brain, placenta and human embryonic kidney cells) and an insect: an activator is present in soluble extracts of abdominal intersegmental muscle from Manduca sexta. Activation is ATP and concentration dependent. There is no stimulation of human red cell-derived 20S proteasome by the Manduca activator ruling out 11S regulator in the preparations. Additionally, cross-species activation occurs: the Manduca activator increases the activity of rat skeletal muscle 26S proteasomes and the human placental activator similarly increases the activity of 26S proteasomes prepared from muscles from Manduca sexta. Finally, there is no evidence for other ATPases in the activator complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006903903534
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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