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Halalkalibacterium halodurans

ABSTRACT: Response of Bacillus halodurans C-125 wild-type and OLE-OAP knockout cells to acute ethanol stress

PROVIDER: PRJNA149331 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR359043_1.fastq.gz	Fastqsanger.gz
	SRR359043_2.fastq.gz	Fastqsanger.gz
	SRR359044_1.fastq.gz	Fastqsanger.gz
	SRR359044_2.fastq.gz	Fastqsanger.gz
	SRR359045_1.fastq.gz	Fastqsanger.gz

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Response of Bacillus halodurans C-125 wild-type and OLE-OAP knockout cells to acute ethanol stress

Project description:OLE RNA (Ornate, Large, Extremophilic RNA) is a large, noncoding RNA from extremophilic and/or anaerobic Firmicutes that binds to an integral membrane protein (OAP, OLE-Associated Protein) and localizes to the cell membrane. It is highly abundant in cells, and knockouts show increased sensitivity to short-chain alcohols, especially ethanol. We treated Bacillus halodurans C-125 cells (both wild-type and OLE-OAP knockouts) with 5% (v/v) ethanol for 3 hours to determine differences in their response to this stress. There are almost no significant differences between cells before ethanol stress, while after ethanol stress a small number (~40) genes show differences in expression between the two strains. These genes show little connection between their function, however, leading us to conclude that the majority of differential adaptation in kncokouts may occur at an earlier time or at the post-trancriptional level. These data also serve as a reference for a Gram-positive alkaliphile's response to acute ethanol stress. Examination of wild-type and OLE-OAP knockout cells before and after ethanol stress, in duplicate (8 samples total)

2012-06-15 | E-GEOD-33303 | biostudies-arrayexpress

Response of Bacillus halodurans C-125 wild-type and OLE-OAP knockout cells to acute ethanol stress

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Recombinant acetylxylan esterase of Halalkalibacterium halodurans NAH-Egypt: molecular and biochemical study.

Project description:Acetylxylan esterase plays a crucial role in xylan hydrolysis as the acetyl side-groups restrict endoxylanase action by stearic hindrance. In this study, an acetylxylan esterase (AXE-HAS10: 960 bp & 319 a.a) putative ORF from Halalkalibacterium halodurans NAH-Egypt was extensively studied through heterologous overexpression in Escherichia coli, biochemical characterization, and structural modeling. The AXE-HAS10 tertiary structure was predicted by the Local Meta Threading Server. AXE-HAS10 belongs to the carbohydrate esterase Family 7. Purified to homogeneity AXE-HAS10 showed specific activity (36.99 U/mg), fold purification (11.42), and molecular mass (41.39 kDa). AXE-HAS10 showed optimal pH (8.5) and temperature (40 oC). After 15 h of incubation at pH 7.0-9.0, AXE-HAS10 maintained 100% activity. After 120 min at 35 and 40 oC, the retained activity was 80 and 50%, respectively. At 10 mM Mn2+, Fe3+, K+, and Ca2+ after 30 min, retained activity was 329 ± 15, 212 ± 5.2, 123 ± 1.4, and 120 ± 3.0%, respectively. After 30 min of preincubation with triton x-100, SDS, and CTAB at 0.1% (v/v), the retained activity was 150 ± 19, 88 ± 4, and 82 ± 7%, respectively. At 6.0 M NaCl after 30 min, retained activity was 58%. A 1.44-fold enhancement of beechwood xylan hydrolysis was achieved by AXE-HAS10 and Penicillium chrysogenum DSM105774 β-xylanase concurrently. Present data underpins AXE-HAS10 as a promising AXE for industrial exploitation.

| S-EPMC9606172 | biostudies-literature

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