Dataset Information

Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis

ABSTRACT: Aggregation is a sequence-specific process, nucleated by short aggregation prone regions (APR) that can be exploited to induce aggregation of proteins containing the same APR. Here we find that most APRs are unique within a proteome, but that a small minority of APRs occur in many proteins. When aggregation is nucleated in bacteria by such frequently occurring APRs, it leads to massive and lethal inclusion body formation containing a large number of proteins. Build-up of bacterial resistance against these peptides is slow. In addition, the approach is effective against drug-resistant clinical isolates of E. coli and A. baumannii, reducing bacterial load in a murine bladder infection model. Our results indicate that redundant APRs are weak points of bacterial protein homeostasis and that targeting these may be an attractive antibacterial strategy.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Escherichia Coli

SUBMITTER: Ladan Khodaparast

LAB HEAD: Joost Schymkowitz

PROVIDER: PXD008685 | Pride | 2018-03-05

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	20160121_laleh_ladan_sample_1.raw (F020863).mzid_20160121_laleh_ladan_sample_1.raw_(F020863).pride.mgf.gz	Mzid
	20160121_laleh_ladan_sample_1.raw (F020863).pride.mztab.gz	Mztab
	20160121_laleh_ladan_sample_1.rawF020863.mzid.gz	Mzid
	20160121_laleh_ladan_sample_1.rawF020863.mzid_20160121_laleh_ladan_sample_1.raw_F020863.MGF	Mzid
	20171003_laleh_ladan_sample_003 (F025043).mzid_20171003_laleh_ladan_sample_003_(F025043).pride.mgf.gz	Mzid

Items per page:

1 - 5 of 234

Publications

Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis.

Khodaparast Ladan L Khodaparast Laleh L Gallardo Rodrigo R Louros Nikolaos N NN Michiels Emiel E Ramakrishnan Reshmi R Ramakers Meine M Claes Filip F Young Lydia L Shahrooei Mohammad M Wilkinson Hannah H Desager Matyas M Mengistu Tadesse Wubishet W Nilsson K Peter R KPR Hammarström Per P Aertsen Abram A Carpentier Sebastien S Van Eldere Johan J Rousseau Frederic F Schymkowitz Joost J

Nature communications 20180228 1

Aggregation is a sequence-specific process, nucleated by short aggregation-prone regions (APRs) that can be exploited to induce aggregation of proteins containing the same APR. Here, we find that most APRs are unique within a proteome, but that a small minority of APRs occur in many proteins. When aggregation is nucleated in bacteria by such frequently occurring APRs, it leads to massive and lethal inclusion body formation containing a large number of proteins. Buildup of bacterial resistance ag ...[more]

PMID: 29491361

Dataset Information

Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis

Dataset's files

Publications

Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Similar Datasets

Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis, part 2
2018-03-05 | PXD008701 | Pride

Apical anchorage and stabilization of subpellicular microtubules by apical polar ring ensures Plasmodium ookinete infection in mosquito
2022-11-18 | PXD038209 |

Heat and pressure resistance relates to protein folding and aggregation
2020-01-27 | PXD011023 | Pride

LC-MS/MS of dithiothreitol-extracted proteins from the insect fungal pathogen Beauveria bassiana hyphal bodies (in vivo blastospores)
2017-01-04 | PXD004544 | Pride

human follicular fluid lc-ms/ms
2018-10-26 | PXD003340 | Pride

Transcriptomics of the Avian Immune Response in Hypothalamus, Spleen, and Red Blood Cells using RNA-seq
2019-07-17 | GSE121348 | GEO

Antibody-free multiplex measurement of 23 human cytokines in primary cell culture secretome using targeted multiple reaction monitoring mass spectrometry
2020-02-19 | PXD015407 | Pride

Braveheart is a long non-coding RNA necessary for cardiac lineage commitment
2013-01-30 | E-GEOD-39656 | biostudies-arrayexpress

Quantitative proteomics of maize roots treated with a novel protein hydrolase: comparative study with transcriptomics highlights the molecular mechanisms responsive to biostimulants
2020-11-16 | PXD017781 | Pride