Send to

Choose Destination
See comment in PubMed Commons below
J Biol Chem. 1998 Dec 11;273(50):33825-34.

Molecular cloning, characterization, and dynamics of rat formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein.

Author information

  • 1Department of Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.


A peripherally associated 58-kDa Golgi protein (58K) of unknown function has been previously described (Bloom, G. S., and Brashear, T. A. (1989) J. Biol. Chem. 264, 16083-16092). To molecularly characterize 58K, we used a monoclonal anti-58K antibody (monoclonal antibody 58K-9) to screen a rat liver cDNA expression library. Positive clones were isolated, characterized, and partially sequenced. The obtained sequences show a high level of identity with sequences of porcine formiminotransferase cyclodeaminase (FTCD), suggesting that 58K is rat FTCD. Rat FTCD is structurally similar to porcine FTCD, a metabolic enzyme involved in conversion of histidine to glutamic acid, and exists in dimeric, tetrameric, and octameric complexes resistant to proteolysis. To define parameters of FTCD association with the Golgi, comparison of its behavior with various Golgi and ER-to-Golgi intermediate compartment marker proteins was examined under specific conditions. The results show that extraction parameters of FTCD are similar to those of GM130, a tightly associated Golgi matrix protein. FTCD appears to be a dynamic component of the Golgi, and a proportion of FTCD molecules cycle between the Golgi and earlier compartments of the secretory pathway. FTCD remains associated with Golgi fragments during microtubule disruption and is not released into cytosol during brefeldin A treatment. Instead, FTCD relocates from the Golgi, but the time course of its redistribution is distinct from that of mannosidase II relocation. FTCD is already dispersed into small punctate structures at a time when mannosidase II is still largely localized to Golgi structures. FTCD is not observed in tubules originating from the Golgi and containing mannosidase II. Instead, it appears to redistribute in small vesicles arranged in a linear "pearls on a string" pattern. These results suggest that FTCD relocation is temporally and spatially distinct from mannosidase II relocation and that FTCD provides a novel marker to study Golgi dynamics.

[PubMed - indexed for MEDLINE]
Free full text

LinkOut - more resources

Full Text Sources

Molecular Biology Databases

PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Write to the Help Desk