Feedback regulation of small RNA processing by the cleavage product. Issue 8 (3rd August 2019)
- Record Type:
- Journal Article
- Title:
- Feedback regulation of small RNA processing by the cleavage product. Issue 8 (3rd August 2019)
- Main Title:
- Feedback regulation of small RNA processing by the cleavage product
- Authors:
- Durica-Mitic, Svetlana
Görke, Boris - Abstract:
- ABSTRACT: Many bacterial small RNAs (sRNAs) are processed resulting in variants with roles potentially distinct from the primary sRNAs. In Enterobacteriaceae sRNA GlmZ activates expression of glmS by base-pairing when the levels of glucosamine-6-phosphate (GlcN6P) are low. GlmS synthesizes GlcN6P, which is required for cell envelope biosynthesis. When dispensable, GlmZ is cleaved by RNase E in the base-pairing sequence. Processing requires protein RapZ, which binds GlmZ and recruits RNase E by interaction. Cleavage is counteracted by the homologous sRNA GlmY, which accumulates upon GlcN6P scarcity and sequesters RapZ. Here, we report a novel role for a processed sRNA. We observed that processing of GlmZ is never complete in vivo . Even upon RapZ overproduction, a fraction of GlmZ remains full-length, while the 5ʹ cleavage product (GlmZ*) accumulates. GlmZ* retains all elements required for RapZ binding. Accordingly, GlmZ* can displace full-length GlmZ from RapZ and counteract processing in vitro . To mimic GlmZ* in vivo, sRNA chimeras were employed consisting of foreign 3ʹ ends including a terminator fused to the 3ʹ end of GlmZ*. In vitro, these chimeras perform indistinguishable from GlmZ*. Expression of the chimeras in vivo inhibited processing of endogenous GlmZ, causing moderate upregulation of GlmS synthesis. Hence, accumulation of GlmZ* prevents complete GlmZ turnover. This mechanism may serve to adjust a robust glmS basal expression level that is buffered againstABSTRACT: Many bacterial small RNAs (sRNAs) are processed resulting in variants with roles potentially distinct from the primary sRNAs. In Enterobacteriaceae sRNA GlmZ activates expression of glmS by base-pairing when the levels of glucosamine-6-phosphate (GlcN6P) are low. GlmS synthesizes GlcN6P, which is required for cell envelope biosynthesis. When dispensable, GlmZ is cleaved by RNase E in the base-pairing sequence. Processing requires protein RapZ, which binds GlmZ and recruits RNase E by interaction. Cleavage is counteracted by the homologous sRNA GlmY, which accumulates upon GlcN6P scarcity and sequesters RapZ. Here, we report a novel role for a processed sRNA. We observed that processing of GlmZ is never complete in vivo . Even upon RapZ overproduction, a fraction of GlmZ remains full-length, while the 5ʹ cleavage product (GlmZ*) accumulates. GlmZ* retains all elements required for RapZ binding. Accordingly, GlmZ* can displace full-length GlmZ from RapZ and counteract processing in vitro . To mimic GlmZ* in vivo, sRNA chimeras were employed consisting of foreign 3ʹ ends including a terminator fused to the 3ʹ end of GlmZ*. In vitro, these chimeras perform indistinguishable from GlmZ*. Expression of the chimeras in vivo inhibited processing of endogenous GlmZ, causing moderate upregulation of GlmS synthesis. Hence, accumulation of GlmZ* prevents complete GlmZ turnover. This mechanism may serve to adjust a robust glmS basal expression level that is buffered against fluctuations in RapZ availability. … (more)
- Is Part Of:
- RNA biology. Volume 16:Issue 8(2019)
- Journal:
- RNA biology
- Issue:
- Volume 16:Issue 8(2019)
- Issue Display:
- Volume 16, Issue 8 (2019)
- Year:
- 2019
- Volume:
- 16
- Issue:
- 8
- Issue Sort Value:
- 2019-0016-0008-0000
- Page Start:
- 1055
- Page End:
- 1065
- Publication Date:
- 2019-08-03
- Subjects:
- Small RNA GlmZ -- RNase E -- adaptor protein RapZ -- RNA processing -- feedback regulation
RNA -- Periodicals
Molecular biology -- Periodicals
Molecular biology
RNA
Periodicals
572.8805 - Journal URLs:
- http://www.tandfonline.com/loi/krnb ↗
http://www.landesbioscience.com/journals/rnabiology/ ↗
http://www.tandfonline.com/ ↗ - DOI:
- 10.1080/15476286.2019.1612693 ↗
- Languages:
- English
- ISSNs:
- 1547-6286
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 7993.991300
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 18618.xml