The role of the Aspergillus nidulans high mobility group B protein HmbA, the orthologue of Saccharomyces cerevisiae Nhp6p

The mammalian HMGB1 is a high-mobility-group B protein, which is both an architectural and functional element of chromatin. Nhp6p, the extensively studied fungal homologue of HMGB1 in Saccharomyces cerevisiae has pleiotropic physiological functions. Despite the existence of Nhp6p orthologues in filamentous ascomycetes, little is known about their physiological roles besides their contribution to sexual development. Here we study the function of HmbA, the Aspergillus nidulans orthologue of Nhp6p. We show that HmbA influences the utilization of various carbon- and nitrogen sources, stress tolerance, secondary metabolism, hyphae elongation and maintenance of polarized growth. Additionally, by conducting heterologous expression studies, we demonstrate that HmbA and Nhp6p are partially interchangeable. HmbA restores SNR6 transcription and fitness of nhp6A Delta B Delta mutant and reverses its heat sensitivity. Nhp6Ap complements several phenotypes of hmbA Delta, including ascospore formation, utilization of various carbon- and nitrogen-sources, radial growth rate, hypha elongation by polarized growth. However, Nhp6Ap does not complement sterigmatocystin production in a hmbA Delta strain. Finally, we also show that HmbA is necessary for the normal expression of the endochitinase chiA, a cell wall re-modeller that is pivotal for the normal mode of maintenance of polar growth.

Automated summary

In this study, the function of HmbA, the Aspergillus nidulans orthologue of Nhp6p, was investigated. It was found that HmbA plays important roles in various physiological processes, such as carbon and nitrogen source utilization, stress tolerance, secondary metabolism, hyphae elongation, and maintenance of polarized growth. The study also demonstrated partial interchangeability between HmbA and Nhp6p.