Abstract:
:LamB-LacZ fusion proteins have classically been used in studies of the general secretion pathway of Escherichia coli. Here we describe how increasing signal sequence hydrophobicity routes LamB-LacZ Hyb42-1 to the signal recognition particle (SRP) pathway. Secretion of this hydrophobic fusion variant (H*LamB-LacZ) was reduced in the absence of fully functional Ffh and Ffs, and the translocator jamming caused by Hyb42-1 was prevented by efficient delivery of the fusion to the periplasm. Finally, we found that in the absence of the ribosome-associated chaperone, trigger factor (Tig), LamB-LacZ localized to the periplasm in a SecA-dependent, SRP-independent fashion. Collectively, our results provide compelling in vivo evidence that there is an SRP-dependent cotranslational targeting mechanism in E. coli and argue against a role for trigger factor in pathway discrimination.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Bowers CW,Lau F,Silhavy TJdoi
10.1128/jb.185.19.5697-5705.2003keywords:
subject
Has Abstractpub_date
2003-10-01 00:00:00pages
5697-705issue
19eissn
0021-9193issn
1098-5530journal_volume
185pub_type
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更新日期:1994-07-01 00:00:00
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pub_type: 杂志文章
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