Abstract:
:To investigate the role of the prevacuolar secretion pathway in the trafficking of vacuolar proteins in Candida albicans, the C. albicans homolog of the Saccharomyces cerevisiae vacuolar protein sorting gene VPS4 was cloned and analyzed. Candida albicans VPS4 encodes a deduced AAA-type ATPase that is 75.6% similar to S. cerevisiae Vps4p, and plasmids bearing C. albicans VPS4 complemented the abnormal vacuolar morphology and carboxypeptidase missorting in S. cerevisiae vps4 null mutants. Candida albicans vps4Delta null mutants displayed a characteristic class E vacuolar morphology and multilamellar structures consistent with an aberrant prevacuolar compartment. The C. albicans vps4Delta mutant degraded more extracellular bovine serum albumin than did wild-type strains, which implied that this mutant secreted more extracellular protease activity. These phenotypes were complemented when a wild-type copy of VPS4 was reintroduced into its proper locus. Using a series of protease inhibitors, the origin of this extracellular protease activity was identified as a serine protease, and genetic analyses using a C. albicans vps4Deltaprc1Delta mutant identified this missorted vacuolar protease as carboxypeptidase Y. Unexpectedly, C. albicans Sap2p was not detected in culture supernatants of the vps4Delta mutants. These results indicate that C. albicans VPS4 is required for vacuolar biogenesis and proper sorting of vacuolar proteins.
journal_name
FEMS Yeast Resjournal_title
FEMS yeast researchauthors
Lee SA,Jones J,Khalique Z,Kot J,Alba M,Bernardo S,Seghal A,Wong Bdoi
10.1111/j.1567-1364.2007.00253.xsubject
Has Abstractpub_date
2007-09-01 00:00:00pages
973-85issue
6eissn
1567-1356issn
1567-1364pii
FYR253journal_volume
7pub_type
杂志文章abstract::The yeast Pichia pastoris is a widely used host organism for heterologous protein production. One of the basic steps for strain improvement is to ensure a sufficient level of transcription of the heterologous gene, based on promoter strength and gene copy number. To date, high-copy-number integrants of P. pastoris are...
journal_title:FEMS yeast research
pub_type: 杂志文章
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journal_title:FEMS yeast research
pub_type: 杂志文章
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journal_title:FEMS yeast research
pub_type: 杂志文章
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journal_title:FEMS yeast research
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journal_title:FEMS yeast research
pub_type: 杂志文章
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pub_type: 杂志文章
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abstract::Amylases are used in a variety of industries that have a specific need for alternative enzymes capable of hydrolysing raw starch. Five α-amylase and five glucoamylase-encoding genes were expressed in the Saccharomyces cerevisiae Y294 laboratory strain to select for recombinant strains that best hydrolysed raw corn sta...
journal_title:FEMS yeast research
pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:FEMS yeast research
pub_type: 杂志文章
doi:10.1093/femsyr/foy058
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journal_title:FEMS yeast research
pub_type: 杂志文章
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journal_title:FEMS yeast research
pub_type: 杂志文章
doi:10.1093/femsyr/fov097
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journal_title:FEMS yeast research
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journal_title:FEMS yeast research
pub_type: 杂志文章
doi:10.1016/j.femsyr.2004.11.003
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pub_type: 杂志文章
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journal_title:FEMS yeast research
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journal_title:FEMS yeast research
pub_type: 杂志文章
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journal_title:FEMS yeast research
pub_type: 杂志文章
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abstract::Abstract Zinc is an essential micronutrient, and yet it can be toxic when present in excess. Zinc acquisition and distribution are dependent on tightly controlled transport of Zn(2+) ions. Schizosaccharomyces pombe represents a second eukaryotic model to study cellular metal homeostasis. In several ways its micronutri...
journal_title:FEMS yeast research
pub_type: 杂志文章
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journal_title:FEMS yeast research
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journal_title:FEMS yeast research
pub_type: 杂志文章
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journal_title:FEMS yeast research
pub_type: 杂志文章
doi:10.1111/j.1567-1364.2009.00565.x
更新日期:2009-12-01 00:00:00
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journal_title:FEMS yeast research
pub_type: 杂志文章
doi:10.1016/j.femsyr.2004.09.002
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