Electron microscopy study of GroEL chaperonin: different views of the aggregate appear as a function of cell growth temperature.
We have studied two members of the family of morphogenetic factors or chaperonins, the GroEL-like factors from Escherichia coli and Bacillus subtilis, in order to determine the possible structural basis of their related function in promoting the correct and efficient assembly of biological oligomers. The main objective of this work has been to study by transmission electron microscopy the possible changes that these factors may undergo when subjected to a number of different conditions such as changes in temperature in vivo and in pH in vitro. We applied both rotational and multivariate statistical analyses of single particles to images of GroEl-like aggregates from the two bacteria. The most striking result is the finding of two distinct "front views" of these aggregates, from both E. coli and B. subtilis. One view, which has not been described earlier, shows a sixfold symmetry and is most abundant at growing temperatures below 37 degrees C. After heat shock, a view showing seven morphological units becomes dominant. On the basis of our analysis it is clear that GroEL-like morphogenetic factors from two unrelated bacteria such as E. coli and B. subtilis present two distinct views: one sixfold and the other sevenfold. Their relative percentage of appearance is related to the temperature at which the cells were grown and also to the storage conditions (pH).
Carazo
J M
JM
Centro Nacional de Biotecnología, CSIC, Universidad Autónoma, Madrid, Spain.
Marco
S
S
Abella
G
G
Carrascosa
J L
JL
Secilla
J P
JP
Muyal
M
M
D001412:Bacillus subtilis / Q000254:growth & development; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000648:ultrastructure*; D002455:Cell Division; D018834:Chaperonin 60; D004926:Escherichia coli / Q000254:growth & development; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000648:ultrastructure*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008854:Microscopy, Electron; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins