NblA from Anabaena sp PCC 7120 is a mostly alpha-helical protein undergoing reversible trimerization in solution

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Item Type:	Article
Title:	NblA from Anabaena sp PCC 7120 is a mostly alpha-helical protein undergoing reversible trimerization in solution
Creators Name:	Strauss, H., Misselwitz, R., Labudde, D., Nicklisch, S. and Baier, K.
Abstract:	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.
Keywords:	Analytical Ultracentrifugation, Chlorosis, Cyanobacteria, NblA, Phycobilisome
Source:	European Journal of Biochemistry
ISSN:	0014-2956
Publisher:	Blackwell Publishing
Volume:	269
Number:	18
Page Range:	4617-4624
Date:	1 January 2002
Official Publication:	https://doi.org/10.1046/j.1432-1033.2002.03161.x
PubMed:	View item in PubMed

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