The Salmonella type III secretion system inner rod protein PrgJ is partially folded.

The type III secretion system (T3SS) is essential in the pathogenesis of many bacteria. The inner rod is important in the assembly of the T3SS needle complex. However, the atomic structure of the inner rod protein is currently unknown. Based on computational methods, others have suggested that the S...

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Main Authors: Zhong, D, Lefebre, M, Kaur, K, McDowell, M, Gdowski, C, Jo, S, Wang, Y, Benedict, S, Lea, S, Galan, J, De Guzman, R
Format: Journal article
Language:English
Published: 2012
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author Zhong, D
Lefebre, M
Kaur, K
McDowell, M
Gdowski, C
Jo, S
Wang, Y
Benedict, S
Lea, S
Galan, J
De Guzman, R
author_facet Zhong, D
Lefebre, M
Kaur, K
McDowell, M
Gdowski, C
Jo, S
Wang, Y
Benedict, S
Lea, S
Galan, J
De Guzman, R
author_sort Zhong, D
collection OXFORD
description The type III secretion system (T3SS) is essential in the pathogenesis of many bacteria. The inner rod is important in the assembly of the T3SS needle complex. However, the atomic structure of the inner rod protein is currently unknown. Based on computational methods, others have suggested that the Salmonella inner rod protein PrgJ is highly helical, forming a folded 3 helix structure. Here we show by CD and NMR spectroscopy that the monomeric form of PrgJ lacks a tertiary structure, and the only well-structured part of PrgJ is a short α-helix at the C-terminal region from residues 65-82. Disruption of this helix by glycine or proline mutation resulted in defective assembly of the needle complex, rendering bacteria incapable of secreting effector proteins. Likewise, CD and NMR data for the Shigella inner rod protein MxiI indicate this protein lacks a tertiary structure as well. Our results reveal that the monomeric forms of the T3SS inner rod proteins are partially folded.
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spelling oxford-uuid:a5fe7553-f610-4d32-9508-6ce29e6124bb2022-03-27T02:44:12ZThe Salmonella type III secretion system inner rod protein PrgJ is partially folded.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:a5fe7553-f610-4d32-9508-6ce29e6124bbEnglishSymplectic Elements at Oxford2012Zhong, DLefebre, MKaur, KMcDowell, MGdowski, CJo, SWang, YBenedict, SLea, SGalan, JDe Guzman, RThe type III secretion system (T3SS) is essential in the pathogenesis of many bacteria. The inner rod is important in the assembly of the T3SS needle complex. However, the atomic structure of the inner rod protein is currently unknown. Based on computational methods, others have suggested that the Salmonella inner rod protein PrgJ is highly helical, forming a folded 3 helix structure. Here we show by CD and NMR spectroscopy that the monomeric form of PrgJ lacks a tertiary structure, and the only well-structured part of PrgJ is a short α-helix at the C-terminal region from residues 65-82. Disruption of this helix by glycine or proline mutation resulted in defective assembly of the needle complex, rendering bacteria incapable of secreting effector proteins. Likewise, CD and NMR data for the Shigella inner rod protein MxiI indicate this protein lacks a tertiary structure as well. Our results reveal that the monomeric forms of the T3SS inner rod proteins are partially folded.
spellingShingle Zhong, D
Lefebre, M
Kaur, K
McDowell, M
Gdowski, C
Jo, S
Wang, Y
Benedict, S
Lea, S
Galan, J
De Guzman, R
The Salmonella type III secretion system inner rod protein PrgJ is partially folded.
title The Salmonella type III secretion system inner rod protein PrgJ is partially folded.
title_full The Salmonella type III secretion system inner rod protein PrgJ is partially folded.
title_fullStr The Salmonella type III secretion system inner rod protein PrgJ is partially folded.
title_full_unstemmed The Salmonella type III secretion system inner rod protein PrgJ is partially folded.
title_short The Salmonella type III secretion system inner rod protein PrgJ is partially folded.
title_sort salmonella type iii secretion system inner rod protein prgj is partially folded
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