The PGRS domain is responsible for translocation of PE-PGRS30 to cell poles while the PE and the C-terminal domains localize it to the cell wall

Shweta Chatrath; Vineet Kumar Gupta; Lalit C. Garg

doi:10.1016/j.febslet.2014.01.059

The PGRS domain is responsible for translocation of PE-PGRS30 to cell poles while the PE and the C-terminal domains localize it to the cell wall

Shweta Chatrath, Vineet Kumar Gupta, Lalit C. Garg

Surgery

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Abstract

PE-PGRS proteins localize in the mycobacterial cell wall and the cell wall localization of PE-PGRS33 has been shown to be attributed to its PE domain. In this study, we expressed deletion mutants of PE-PGRS30 in Mycobacterium smegmatis to characterize the role of its domains in protein localization. It was revealed that, apart from the PE domain, the C-terminal domain present in few PE-PGRS proteins carries individual cell wall localization signals. Proteinase K sensitivity assay showed that PE-PGRS30 is exposed on the mycobacterial surface through its PGRS domain. PGRS domain was also shown to be responsible for polar localization of PE-PGRS30.

Original language	English (US)
Pages (from-to)	990-994
Number of pages	5
Journal	FEBS Letters
Volume	588
Issue number	6
DOIs	https://doi.org/10.1016/j.febslet.2014.01.059
State	Published - Mar 18 2014

Bibliographical note

Funding Information:
Financial support from Department of Biotechnology, New Delhi , is acknowledged. The Council of Scientific and Industrial Research, New Delhi, is acknowledged for research fellowship to V.K.G. We thank Mr. K.P. Pandey for his technical assistance.

Keywords

C-terminal domain
Localization
Mycobacterium tuberculosis
PE domain
PE-PGRS30
PGRS domain

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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title = "The PGRS domain is responsible for translocation of PE-PGRS30 to cell poles while the PE and the C-terminal domains localize it to the cell wall",

abstract = "PE-PGRS proteins localize in the mycobacterial cell wall and the cell wall localization of PE-PGRS33 has been shown to be attributed to its PE domain. In this study, we expressed deletion mutants of PE-PGRS30 in Mycobacterium smegmatis to characterize the role of its domains in protein localization. It was revealed that, apart from the PE domain, the C-terminal domain present in few PE-PGRS proteins carries individual cell wall localization signals. Proteinase K sensitivity assay showed that PE-PGRS30 is exposed on the mycobacterial surface through its PGRS domain. PGRS domain was also shown to be responsible for polar localization of PE-PGRS30.",

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author = "Shweta Chatrath and Gupta, {Vineet Kumar} and Garg, {Lalit C.}",

note = "Funding Information: Financial support from Department of Biotechnology, New Delhi , is acknowledged. The Council of Scientific and Industrial Research, New Delhi, is acknowledged for research fellowship to V.K.G. We thank Mr. K.P. Pandey for his technical assistance.",

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AU - Chatrath, Shweta

AU - Gupta, Vineet Kumar

AU - Garg, Lalit C.

N1 - Funding Information: Financial support from Department of Biotechnology, New Delhi , is acknowledged. The Council of Scientific and Industrial Research, New Delhi, is acknowledged for research fellowship to V.K.G. We thank Mr. K.P. Pandey for his technical assistance.

PY - 2014/3/18

Y1 - 2014/3/18

N2 - PE-PGRS proteins localize in the mycobacterial cell wall and the cell wall localization of PE-PGRS33 has been shown to be attributed to its PE domain. In this study, we expressed deletion mutants of PE-PGRS30 in Mycobacterium smegmatis to characterize the role of its domains in protein localization. It was revealed that, apart from the PE domain, the C-terminal domain present in few PE-PGRS proteins carries individual cell wall localization signals. Proteinase K sensitivity assay showed that PE-PGRS30 is exposed on the mycobacterial surface through its PGRS domain. PGRS domain was also shown to be responsible for polar localization of PE-PGRS30.

AB - PE-PGRS proteins localize in the mycobacterial cell wall and the cell wall localization of PE-PGRS33 has been shown to be attributed to its PE domain. In this study, we expressed deletion mutants of PE-PGRS30 in Mycobacterium smegmatis to characterize the role of its domains in protein localization. It was revealed that, apart from the PE domain, the C-terminal domain present in few PE-PGRS proteins carries individual cell wall localization signals. Proteinase K sensitivity assay showed that PE-PGRS30 is exposed on the mycobacterial surface through its PGRS domain. PGRS domain was also shown to be responsible for polar localization of PE-PGRS30.

KW - C-terminal domain

KW - Localization

KW - Mycobacterium tuberculosis

KW - PE domain

KW - PE-PGRS30

KW - PGRS domain

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The PGRS domain is responsible for translocation of PE-PGRS30 to cell poles while the PE and the C-terminal domains localize it to the cell wall

Abstract

Bibliographical note

Keywords

UN SDGs

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