Work

SNAP‐25 is also an iron–sulfur protein

Year: 2008

Type: article

Abstract: SNAP-25 has a cysteine cluster located at its linker domain. In vivo, the cysteine residues in this cluster can be palmitoylated, and the hydrophobic palmitate molecules can target SNAP-25 to the presynaptic membrane. Here, we report that the SNAP-25a expressed in Escherichia coli is also an iron-sulfur protein binding an iron-sulfur cluster using the cysteine residues in its cysteine cluster. Therefore, SNAP-25a uses the same cysteine residues to bind two different prosthetic groups (iron-sulfur cluster and palmitate). Because the binding sites of these two prosthetic groups overlap, we suggest that these two modifications occur at different times, and probably at different places in the cell.

Source: FEBS Letters

DOI: 10.1016/j.febslet.2008.03.028

Authors: Qingqiu Huang, Xinguo Hong, Quan Hao

Institutions: Cornell University, Cornell High Energy Synchrotron Source

Language: English

Topic: Cellular transport and secretion

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institute of General Medical Sciences, National Center for Research Resources

Awards: G1641640346, Macromolecular Diffraction Resource: MacCHESS, Macromolecular Diffraction Resource: MacCHESS