Abstract:
:The TBF-1 is an 11.9-kDa fruiting body specific protein of the Ascomycetes hypogeous fungus Tuber borchii Vittad. found in aqueous extract and the hyphal cell wall. The tbf-1 gene codes a 12-amino acid N-terminal stretch not present in mature protein. This sequence does not match with any homologous signal sequences stored in data banks. To investigate the role of the N-terminus in TBF-1 localization, cDNA was expressed in Saccharomyces cerevisiae under the control of the 3-phosphoglycerate kinase promoter. Like Tuber, yeast also produces and secretes TBF-1 and the foreign protein binds with the cell wall. A signalless mutant protein was constructed; this DeltaTBF-1 was expressed but not exported by yeast. The secretion of TBF-1 was also suppressed using the sec18(ts) yeast mutant strain grown at nonpermissive temperature as host. Thus we demonstrated that the N-terminal 12-amino acid stretch is a noncanonical signal peptide that leads the TBF-1 toward the classical secretory pathway in yeast.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Palma F,Cerigini E,Stocchi Vdoi
10.1111/j.1574-6968.2007.00748.xsubject
Has Abstractpub_date
2007-07-01 00:00:00pages
114-9issue
1eissn
0378-1097issn
1574-6968pii
FML748journal_volume
272pub_type
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