TY - JOUR
T1 - Anomalous dissociative behavior of the major glycosylated component of the cellulosome of clostridium thermocellum
AU - Morgenstern, Ely
AU - Bayer, Edward A.
AU - Lamed, Raphael
PY - 1991/8
Y1 - 1991/8
N2 - The cellulosome of Clostridium thermocellum is a highly cohesive multienzyme complex that is capable of completely solubilizing insoluble cellulose. One of the major cellulosomal components, the glycosylated S1 subunit, is believed to play an important structural role and normally migrates in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an Mr of 210,000. It is shown here that by simply altering the conditions (pH or ionic strength) of the environment prior to electrophoresis, a different migratory profile for S1 emerges, yielding a collection of bands, all of which migrate faster than the parent band. The original electrophoretic behavior of S1 can be reproduced on restoration of the original pH and ionic strength. These results may bear important significance for the physiological role of the S1 subunit in facilitating the observed synergistic action of the other (cellulolytic) components of the cellulosome.
AB - The cellulosome of Clostridium thermocellum is a highly cohesive multienzyme complex that is capable of completely solubilizing insoluble cellulose. One of the major cellulosomal components, the glycosylated S1 subunit, is believed to play an important structural role and normally migrates in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an Mr of 210,000. It is shown here that by simply altering the conditions (pH or ionic strength) of the environment prior to electrophoresis, a different migratory profile for S1 emerges, yielding a collection of bands, all of which migrate faster than the parent band. The original electrophoretic behavior of S1 can be reproduced on restoration of the original pH and ionic strength. These results may bear important significance for the physiological role of the S1 subunit in facilitating the observed synergistic action of the other (cellulolytic) components of the cellulosome.
KW - Cellulosome
KW - Clostridium thermocellum
KW - SDS-PAGE, anamolous migration
KW - cellulase
KW - multienzyme complex
KW - subunit dissociation
UR - http://www.scopus.com/inward/record.url?scp=0026210233&partnerID=8YFLogxK
U2 - 10.1007/BF02921680
DO - 10.1007/BF02921680
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AN - SCOPUS:0026210233
SN - 0273-2289
VL - 30
SP - 129
EP - 136
JO - Applied Biochemistry and Biotechnology
JF - Applied Biochemistry and Biotechnology
IS - 2
ER -