Abstract
Tubulin, the major component of microtubules, has a tendency to lose its ability to assemble or to bind to ligands in a time-dependent process known as "decay," The decay process also causes tubulin to expose sulfhydryl groups and hydrophobic areas. The antimitotic drug phomopsin A strongly protects the tubulin molecule from decay. Here we have studied the interaction of phomopsin A with αβ tubulin and tubulin which has been treated with subtilisin to remove selectively the C-termini of the α and βchains (αsβs). The binding of phomopsin A to αβ tubulin decreases the sulfhydryl titer by approximately 1.0 mol/mol. Selective removal of the peptides from the C-terminal ends does not affect phomopsin A's interaction with tubulin. Moreover, the αsβs tubulin-phomopsin A complex appears to be more stable than the αβ tubulin-phomopsin A complex as determined by the time-dependent increase in exposure of sulfhydryl groups and hydrophobic areas on tubulin. In fact, phomopsin A inhibits the decay process of αsβs tubulin completely. This observation raises the possibility of determining the conformtion of this configuration of tubulin.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 99-105 |
| Number of pages | 7 |
| Journal | Protein Journal |
| Volume | 16 |
| Issue number | 2 |
| State | Published - 1997 |
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Keywords
- Alkylation
- C-terminal domain
- Hydrophobic areas
- Phomopsin A
- Tubulin
ASJC Scopus subject areas
- Biochemistry
- Analytical Chemistry
- Organic Chemistry
- Bioengineering
Cite this
Interaction of phomopsin A with normal and subtilisin-treated bovine brain tubulin. / Chaudhuri, Asish Ray; Ludueña, Richard F.
In: Protein Journal, Vol. 16, No. 2, 1997, p. 99-105.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Interaction of phomopsin A with normal and subtilisin-treated bovine brain tubulin
AU - Chaudhuri, Asish Ray
AU - Ludueña, Richard F.
PY - 1997
Y1 - 1997
N2 - Tubulin, the major component of microtubules, has a tendency to lose its ability to assemble or to bind to ligands in a time-dependent process known as "decay," The decay process also causes tubulin to expose sulfhydryl groups and hydrophobic areas. The antimitotic drug phomopsin A strongly protects the tubulin molecule from decay. Here we have studied the interaction of phomopsin A with αβ tubulin and tubulin which has been treated with subtilisin to remove selectively the C-termini of the α and βchains (αsβs). The binding of phomopsin A to αβ tubulin decreases the sulfhydryl titer by approximately 1.0 mol/mol. Selective removal of the peptides from the C-terminal ends does not affect phomopsin A's interaction with tubulin. Moreover, the αsβs tubulin-phomopsin A complex appears to be more stable than the αβ tubulin-phomopsin A complex as determined by the time-dependent increase in exposure of sulfhydryl groups and hydrophobic areas on tubulin. In fact, phomopsin A inhibits the decay process of αsβs tubulin completely. This observation raises the possibility of determining the conformtion of this configuration of tubulin.
AB - Tubulin, the major component of microtubules, has a tendency to lose its ability to assemble or to bind to ligands in a time-dependent process known as "decay," The decay process also causes tubulin to expose sulfhydryl groups and hydrophobic areas. The antimitotic drug phomopsin A strongly protects the tubulin molecule from decay. Here we have studied the interaction of phomopsin A with αβ tubulin and tubulin which has been treated with subtilisin to remove selectively the C-termini of the α and βchains (αsβs). The binding of phomopsin A to αβ tubulin decreases the sulfhydryl titer by approximately 1.0 mol/mol. Selective removal of the peptides from the C-terminal ends does not affect phomopsin A's interaction with tubulin. Moreover, the αsβs tubulin-phomopsin A complex appears to be more stable than the αβ tubulin-phomopsin A complex as determined by the time-dependent increase in exposure of sulfhydryl groups and hydrophobic areas on tubulin. In fact, phomopsin A inhibits the decay process of αsβs tubulin completely. This observation raises the possibility of determining the conformtion of this configuration of tubulin.
KW - Alkylation
KW - C-terminal domain
KW - Hydrophobic areas
KW - Phomopsin A
KW - Tubulin
UR - http://www.scopus.com/inward/record.url?scp=53249119478&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=53249119478&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:53249119478
VL - 16
SP - 99
EP - 105
JO - Protein Journal
JF - Protein Journal
SN - 1572-3887
IS - 2
ER -