PXD009164-1

PXD009164 is an original dataset announced via ProteomeXchange.

Title	Comparative analysis of homologous aminopeptidase PepN from Mycobacterium tuberculosis and Mycobacterium smegmatis reveals dichotomy of traits
Description	Bacterial pathogens exploit secreted aminopeptidases to modulate host cellular functions. Mycobacterium tuberculosis (Mtb) secretes PepN, a M1 aminopeptidase with N-terminal peptidase and C-terminal ERAP1_C-like domains. In addition to being conserved across Mtb complex, PepNMtb is also homologous (78% amino acids identity) to PepN of M. smegmatis (Msmeg), a non-pathogenic mycobacterium. Despite high homogeneity, PepNMtb and PepNMsmeg exhibit opposing traits thus providing insights into their plausible bacterial/host-specific functions. Our biochemical studies show that, while both PepNs uniformly accumulate across all stages of in vitro growth, unlike Mtb, Msmeg is intolerant to over accumulation of its PepN and hence robustly proteolyzes it. Our proteomic analyses indicate Msmeg also secreting some of its excess PepN into its culture supernatant. In contrast, Mtb does not excessively secrete or proteolyse its over accumulating PepNMtb. Our fractionation studies show Mtb translocating its full length PepNMtb into its membrane and cell wall fractions. Instead, Msmeg accumulates its full length PepNMsmeg in its cytosol, and promotes its cleaved (~40 kDa) form to locate into subcellular fractions. PepNMtb is redundant for Mtb’s in vitro growth and thus Mtb is readily amenable to ΔpepN generation. Opposingly, PepNMsmeg is necessary but not sufficient for Msmeg growth in vitro. Given such disparity, co-immunoprecipitation studies on both PepNs predictably showed divergent interactomes with minimal common hits. In our in vitro infection studies, PepNMtb localizes host endoplasmic reticulum directing us to its potential host-specific role. In summary, our study provides insights into PepNs dichotomy despite them being conserved across pathogenic and non-pathogenic mycobacterial species.
HostingRepository	PRIDE
AnnounceDate	2019-07-29
AnnouncementXML	Submission_2019-07-29_02:09:54.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Saravanan Kumar
SpeciesList	scientific name: Mycobacterium tuberculosis; NCBI TaxID: 1773; scientific name: Mycobacterium smegmatis; NCBI TaxID: 1772;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2018-03-09 09:18:31	ID requested
⏵ 1	2019-07-29 02:09:56	announced
2	2024-10-22 04:43:52	announced	2024-10-22: Updated project metadata.

Sharma N, Aggarwal S, Kumar S, Sharma R, Choudhury K, Singh N, Jayaswal P, Goel R, Wajid S, Yadav AK, Atmakuri K, Comparative analysis of homologous aminopeptidase PepN from pathogenic and non-pathogenic mycobacteria reveals divergent traits. PLoS One, 14(4):e0215123(2019) [pubmed]

curator keyword: Biological

submitter keyword: Aminopeptidase

Mycobacteria

Mass Spectrometry

Metalloenzyme

Mycobacterium smegmatis

Mycobacterium tuberculosis

Tuberculosis

Secretion

Endoplasmic reticulum.

Krishnamohan Atmakuri
contact affiliation	Assistant Professor Ramalingaswami Fellow Translational Health Science and Technology Institute NCR Biotech Science Cluster 3rd Milestone, Faridabad - Gurgaon Expressway PO box # 04 FARIDABAD 121001, India
contact email	atmakrish@thsti.res.in
lab head
Saravanan Kumar
contact affiliation	Application Scientist, Thermo Fisher Sci
contact email	saravanankumar.icgeb@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD009164
     1. Label: PRIDE project
     2. Name: Comparative analysis of homologous aminopeptidase PepN from Mycobacterium tuberculosis and Mycobacterium smegmatis reveals dichotomy of traits