NblA from Anabaena sp. PCC 7120 is a mostly alpha-helical protein undergoing reversible trimerization in solution.
The nblA family of genes encodes for small proteins necessary for the ordered degradation of phycobilisomes under certain stress conditions, a process known as chlorosis. Genes homologous to nblA seem to occur in all phycobilisome-containing organisms. However, to date, no molecular mechanism is known for the action of NblA, nor have the gene products been characterized to understand the physical properties of the molecule and thus help elucidate the mechanism on a structural basis. In this study we report on the first characterization of an NblA-homologous gene product. The chromosomal gene from the cyanobacterium Anabaena sp. PCC 7120 was cloned, heterologously expressed in Escherichia coli and purified to apparent homogeneity. This allowed the protein to be characterized by analytical ultracentrifugation and CD spectroscopy. These experiments show that the NblA protein has a mostly alpha-helical structure, undergoing an association reaction of folded monomers to form trimers in solution. No dimers are detectable.
Strauss
Holger
H
Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany. strauss@fmp-berlin.de
Misselwitz
Rolf
R
Labudde
Dirk
D
Nicklisch
Sabine
S
Baier
Kerstin
K
D017033:Anabaena / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D003080:Cold Temperature; D006358:Hot Temperature; D045524:Phycobilisomes; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence; D014461:Ultracentrifugation
D001426:Bacterial Proteins; D045524:Phycobilisomes