Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-8-24
pubmed:abstractText
The vacuolar hydrolase protease B in Saccharomyces cerevisiae is synthesized as an inactive precursor (Prb1p). The precursor undergoes post-translational modifications while transiting the secretory pathway. In addition to N- and O-linked glycosylations, four proteolytic cleavages occur during the maturation of Prb1p. Removal of the signal peptide by signal peptidase and the autocatalytic cleavage of the large amino-terminal propeptide occur in the endoplasmic reticulum (ER). Two carboxy-terminal cleavages of the post regions occur in the vacuole: the first cleavage is catalyzed by protease A and the second results from autocatalysis. We have isolated a mutant, pbn1-1, that exhibits a defect in the ER processing of Prb1p. The autocatalytic cleavage of the propeptide from Prb1p does not occur and Prb1p is rapidly degraded in the cytosol. PBN1 was cloned and is identical to YCL052c on chromosome III. PBN1 is an essential gene that encodes a novel protein. Pbn1p is predicted to contain a sub-C-terminal transmembrane domain but no signal sequence. A functional HA epitope-tagged Pbn1p fusion localizes to the ER. Pbn1p is N-glycosylated in its amino-terminal domain, indicating a lumenal orientation despite the lack of a signal sequence. Based on these results, we propose that one of the functions of Pbn1p is to aid in the autocatalytic processing of Prb1p.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-1195389, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-1313948, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-1400575, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-1550957, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-1628805, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-17247984, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-17797907, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-1918142, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-2005802, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-2005809, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-2233730, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-2547163, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-2645294, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-2659436, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-2674123, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-2762295, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-2784443, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-3049073, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-3292536, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-3319781, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-3325823, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-4598444, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-6749836, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-6764901, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-7021321, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-7108955, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-7202124, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-7565784, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-7714895, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-7736572, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-8194519, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-8257795, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-8270629, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-8384581, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-8393731, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-8730101, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-8781238, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-8789256, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-8811181, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-8824380, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-8929540, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-9045801, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-9168472, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-9278052, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-9371780, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649520-9409541
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0016-6731
pubmed:author
pubmed:issnType
Print
pubmed:volume
149
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1277-92
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
The PBN1 gene of Saccharomyces cerevisiae: an essential gene that is required for the post-translational processing of the protease B precursor.
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