Secretion of atypical protein substrates by the ESAT-6 secretion system of Staphylococcus aureus.
Secretion of atypical protein substrates by the ESAT-6 secretion system of Staphylococcus aureus.
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DOI:
10.1111/mmi.12395
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发表时间:
2013-11
影响因子:
3.6
通讯作者:
Missiakas D
中科院分区:
文献类型:
--
作者:
Anderson M;Aly KA;Chen YH;Missiakas D
Staphylococcus aureus encodes the specialized ESAT-6 Secretion System (ESS). EsxA and EsxB are secreted by the ESS pathway, and share sequence features of ESAT-6 and CFP-10 of the Type VII Secretion System (T7SS) of Mycobacterium tuberculosis. Unlike ESAT-6 and CFP-10, EsxA and EsxB do not interact. Instead, EsxB associates with a novel substrate, EsxD, and EsxA dimerizes with itself or EsxC (EsaC). Unlike EsxA and EsxB, EsxC and EsxD do not share obvious sequence features of WXG100 proteins nor PE/PPE and Esp families of proteins, all of which belong to the pfam EsxAB clan of mycobacterial T7SS. EsxD carries the C terminal motif YxxxD/E that has been proposed to target T7 substrates for secretion in mycobacteria. Here, we find that deletion, but not amino acid substitutions, in this motif prevent secretion of EsxA and EsxC but not EsxB or EsxD. This is unlike the genetic inactivation of esxA, esxB, esxC or esxD that leads to loss of secretion of all four substrates. Thus, substrate secretion can be uncoupled by deleting the last six amino acids of EsxD. The physical association of EsxC and EsxD with canonical WXG100 proteins suggests that these proteins belong to the EsxAB clan.
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DOI:
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发表时间:
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影响因子:
11.1
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通讯作者:
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DOI:
10.1073/pnas.0504922102
发表时间:
2005-07-26
影响因子:
11.1
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通讯作者:
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