Abstract:
:The role of HoxX in hydrogenase biosynthesis of Alcaligenes eutrophus H16 was re-examined. The previously characterized hoxX deletion mutant HF344 and a newly constructed second hoxX mutant carrying a smaller in-frame deletion were studied. The second mutant was impaired in the activity of both the soluble and the membrane-bound hydrogenase. The two hydrogenase activities were reduced by approximately 50% due to delayed processing of the active-site-containing large subunits, while hydrogenase gene expression was not affected. We conclude that the mutation in mutant HF344 causes polarity resulting in the observed regulatory phenotype of this mutant. The data presented in this report point to an enhancing function of HoxX in the conversion of the soluble hydrogenase and of the membrane-bound hydrogenase large-subunit precursor. Thus, hoxX encodes a member of the Hyp proteins that are required for the formation of active hydrogenase and was accordingly renamed hypX.
journal_name
Arch Microbioljournal_title
Archives of microbiologyauthors
Buhrke T,Friedrich Bdoi
10.1007/s002030050667subject
Has Abstractpub_date
1998-11-01 00:00:00pages
460-3issue
6eissn
0302-8933issn
1432-072Xjournal_volume
170pub_type
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journal_title:Archives of microbiology
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journal_title:Archives of microbiology
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journal_title:Archives of microbiology
pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1981-09-01 00:00:00
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