Type III Secretion of the Salmonella Effector Protein SopE Is Mediated via an N-Terminal Amino Acid Signal and Not an mRNA Sequence
Autor: | M H, Karavolos, A J, Roe, M, Wilson, J, Henderson, J J, Lee, D L, Gally, C M A, Khan |
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Rok vydání: | 2005 |
Předmět: |
Salmonella typhimurium
Untranslated region Five prime untranslated region Amino Acid Motifs Molecular Sequence Data Biology Microbiology Frameshift mutation Bacterial Proteins Bacterial Proteins/chemistry Secretion RNA Messenger/physiology Salmonella typhimurium/physiology Amino Acid Sequence RNA Messenger Frameshift Mutation Molecular Biology Peptide sequence Molecular Biology of Pathogens chemistry.chemical_classification Bacterial Proteins/secretion Bacterial Proteins/genetics Bacterial Proteins/metabolism Effector Gene Expression Regulation Bacterial biochemical phenomena metabolism and nutrition Amino Acid Motifs/physiology Amino acid Protein Transport chemistry Biochemistry Chaperone binding RNA Messenger/chemistry |
Zdroj: | Karavolos, M H, Roe, A J, Wilson, M, Henderson, J, Lee, J J, Gally, D L & Khan, C M A 2005, ' Type III secretion of the Salmonella effector protein SopE is mediated via an N-terminal amino acid signal and not an mRNA sequence ', Journal of Bacteriology, vol. 187, no. 5, pp. 1559-67 . https://doi.org/10.1128/JB.187.5.1559-1567.2005 |
ISSN: | 1098-5530 0021-9193 |
DOI: | 10.1128/jb.187.5.1559-1567.2005 |
Popis: | Type III secretion systems (TTSS) are virulence-associated components of many gram-negative bacteria that translocate bacterial proteins directly from the bacterial cytoplasm into the host cell. The Salmonella translocated effector protein SopE has no consensus cleavable amino-terminal secretion sequence, and the mechanism leading to its secretion through the Salmonella pathogenicity island 1 (SPI-1) TTSS is still not fully understood. There is evidence from other bacteria which suggests that the TTSS signal may reside within the 5′ untranslated region (UTR) of the mRNA of secreted effectors. We investigated the role of the 5′ UTR in the SPI-1 TTSS-mediated secretion of SopE using promoter fusions and obtained data indicating that the mRNA sequence is not involved in the secretion process. To clarify the proteinaceous versus RNA nature of the signal, we constructed frameshift mutations in the amino-terminal region of SopE of Salmonella enterica serovar Typhimurium SL1344. Only constructs with the native amino acid sequence were secreted, highlighting the importance of the amino acid sequence versus the mRNA sequence for secretion. Additionally, we obtained frameshift mutation data suggesting that the first 15 amino acids are important for secretion of SopE independent of the presence of the chaperone binding site. These data shed light on the nature of the signal for SopE secretion and highlight the importance of the amino-terminal amino acids for correct targeting and secretion of SopE via the SPI-1-encoded TTSS during host cell invasion. |
Databáze: | OpenAIRE |
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