LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Family |
| Description | Protein folding is thought to be the sole result of properties inherent in polypeptide primary sequences. Sometimes, however, additional proteins are required to mediate correct folding and subsequent oligomer assembly [ ]. These `helpers', or chaperones, bind to specific protein surfaces, preventing incorrect folding and formation of non-functional structures [].The tailless complex polypeptide 1 (TCP-1) is a highly structurally conserved molecular chaperone located in the cytosol [ ]. The protein has also been shown to bind to Golgi membranes and to microtubules, this latter property suggesting a role in mitotic spindle formation in dividing cells (especially in sperm, where it is highly abundant) []. TCP-1 forms a double ring structure, similar to the 10kDa and 60kDa chaperonins, with 6-8 subunits per ring. The amino acid sequence is significantly similar to the 60kDa chaperonin, and to TF55, a chaperone from the archaebacterium Sulfolobus shibatae []. |
| Short Name | Chaperone_TCP-1 |
