Abstract:
:Bacterial carboxyl-terminal processing proteases (CTPs) are widely conserved and have been linked to important processes including signal transduction, cell wall metabolism, and virulence. However, the features that target proteins for CTP-dependent cleavage are unclear. Studies of the Escherichia coli CTP Prc suggested that it cleaves proteins with non-polar and/or structurally unconstrained C-termini, but it is not clear if this applies broadly. Pseudomonas aeruginosa has a divergent CTP, CtpA, which is required for virulence. CtpA works in complex with the outer membrane lipoprotein LbcA to degrade cell wall hydrolases. Here, we investigated if the C-termini of two non-homologous CtpA substrates are important for their degradation. We determined that these substrates have extended C-termini, compared to their closest E. coli homologs. Removing seven amino acids from these extensions was sufficient to reduce their degradation by CtpA both in vivo and in vitro Degradation of one truncated substrate was restored by adding the C-terminus from the other, but not by adding an unrelated sequence. However, modification of the C-terminus of non-substrates, by adding the C-terminal amino acids from a substrate, did not cause their degradation by CtpA. Therefore, the C-termini of CtpA substrates are required but not sufficient for their efficient degradation. Although C-terminal truncated substrates were protected from degradation, they still associated with the LbcA•CtpA complex in vivo Therefore, degradation of a protein by CtpA requires a C-terminal-independent interaction with the LbcA•CtpA complex, followed by C-terminal-dependent degradation, perhaps because CtpA normally initiates cleavage at a C-terminal site.IMPORTANCE Carboxyl-terminal processing proteases (CTPs) are found in all three domains of life, but exactly how they work is poorly understood, including how they recognize substrates. Bacterial CTPs have been associated with virulence, including CtpA of Pseudomonas aeruginosa, which works in complex with the outer membrane lipoprotein LbcA to degrade potentially dangerous peptidoglycan hydrolases. We report an important advance by revealing that efficient degradation by CtpA requires at least two separable phenomena, and that one of them depends on information encoded in the substrate C-terminus. A C-terminal-independent association with the LbcA•CtpA complex is followed by C-terminal-dependent cleavage by CtpA. Increased understanding of how CTPs target proteins is significant, due to their links to virulence, peptidoglycan remodeling, and other important processes.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Chung S,Darwin AJdoi
10.1128/JB.00174-20subject
Has Abstractpub_date
2020-06-01 00:00:00eissn
0021-9193issn
1098-5530pii
JB.00174-20pub_type
杂志文章abstract::The location of the Escherichia coli K-12 genes determining or regulating glutamate transport, and the location of the gene determining glutamate decarboxylase synthesis, were established by conjugation. The ability to grow on glutamate as the sole source of carbon and energy was used to select for glutamate transport...
journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.93.4.1409-1415.1967
更新日期:1967-04-01 00:00:00
abstract::The cysteine-rich envelope proteins of the elementary body form of chlamydiae are thought to be located in the outer membrane on the basis of their insolubility in the weak anionic detergent N-lauryl sarcosinate (Sarkosyl). We found, however, that the insolubility of the small (EnvA) and the large (EnvB) cysteine-rich...
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doi:10.1128/jb.177.4.877-882.1995
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doi:10.1128/jb.182.7.2010-2017.2000
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doi:10.1128/JB.131.3.789-794.1977
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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pub_type: 杂志文章
doi:10.1128/JB.180.21.5689-5696.1998
更新日期:1998-11-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1980-07-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.140.2.738-741.1979
更新日期:1979-11-01 00:00:00
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pub_type: 杂志文章
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.174.7.2416-2417.1992
更新日期:1992-04-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:2002-10-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.173.6.2053-2060.1991
更新日期:1991-03-01 00:00:00
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pub_type: 杂志文章
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更新日期:2004-08-01 00:00:00
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更新日期:2000-06-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.169.11.5298-5300.1987
更新日期:1987-11-01 00:00:00
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pub_type: 杂志文章
doi:10.1128/jb.174.7.2267-2272.1992
更新日期:1992-04-01 00:00:00
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journal_title:Journal of bacteriology
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更新日期:1988-01-01 00:00:00
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更新日期:1975-09-01 00:00:00
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更新日期:1982-09-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.98.3.943-946.1969
更新日期:1969-06-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1987-04-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.174.7.2323-2331.1992
更新日期:1992-04-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:2009-04-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.174.2.492-498.1992
更新日期:1992-01-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1997-08-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.140.1.37-42.1979
更新日期:1979-10-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.176.14.4328-4337.1994
更新日期:1994-07-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.153.2.1038-1044.1983
更新日期:1983-02-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.175.22.7430-7440.1993
更新日期:1993-11-01 00:00:00