Previous Article | Next Article ![]()
Eukaryotic Cell, December 2006, p. 2161-2173, Vol. 5, No. 12
1535-9778/06/$08.00+0 doi:10.1128/EC.00253-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
,
and
N. Louise Glass*
Department of Plant and Microbial Biology, The University of California, Berkeley, California 94720-3102
Received 9 August 2006/ Accepted 7 September 2006
Nonself recognition during somatic growth is an essential and ubiquitous phenomenon in both prokaryotic and eukaryotic species. In filamentous fungi, nonself recognition is also important during vegetative growth. Hyphal fusion between genetically dissimilar individuals results in rejection of heterokaryon formation and in programmed cell death of the fusion compartment. In filamentous fungi, such as Neurospora crassa, nonself recognition and heterokaryon incompatibility (HI) are regulated by genetic differences at het loci. In N. crassa, mutations at the vib-1 locus suppress nonself recognition and HI mediated by genetic differences at het-c/pin-c, mat, and un-24/het-6. vib-1 is a homolog of Saccharomyces cerevisiae NDT80, which is a transcriptional activator of genes during meiosis. For this study, we determined that vib-1 encodes a nuclear protein and showed that VIB-1 localization varies during asexual reproduction and during HI. vib-1 is required for the expression of genes involved in nonself recognition and HI, including pin-c, tol, and het-6; all of these genes encode proteins containing a HET domain. vib-1 is also required for the production of downstream effectors associated with HI, including the production of extracellular proteases upon carbon and nitrogen starvation. Our data support a model in which mechanisms associated with starvation and nonself recognition/HI are interconnected. VIB-1 is a major regulator of responses to nitrogen and carbon starvation and is essential for the expression of genes involved in nonself recognition and death in N. crassa.
Published ahead of print on 29 September 2006.
Supplemental material for this article may be found at http://ec.asm.org/.
Present address: Department of Chemistry & Biochemistry, University of California at Los Angeles, 607 Charles E. Young Drive E., Los Angeles, CA 90095.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»