Abstract:
:E. coli GroEL chaperonin monomers, isolated after urea-induced dissociation of GroEL14, undergo cold denaturation below 5 degrees C. Above 5 degrees C, these monomers undergo MgATP-dependent self-assembly. We have demonstrated a conformational transition at 0 degree C induced by interaction of monomeric GroEL with adenine nucleotides. This conformation has a dramatically decreased Stokes radius and enhanced resistance to trypsin but it is slightly less compact than the conformation of monomers at 23 degrees C in the absence of MgATP and it is not capable of spontaneous self-assembly. A second, temperature-dependent conformational change with a transition at about 5 degrees C is required for GroEL to undergo oligomerization.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Lissin NM,Hemmingsen SMdoi
10.1016/0014-5793(93)81528-8subject
Has Abstractpub_date
1993-06-07 00:00:00pages
41-4issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(93)81528-8journal_volume
324pub_type
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