1994
DOI: 10.1128/jb.176.16.5005-5010.1994
|View full text |Cite
|
Sign up to set email alerts
|

micF antisense RNA has a major role in osmoregulation of OmpF in Escherichia coli

Abstract: micF RNA, produced from a multicopy plasmid, was originally shown to be a major factor in negative osmoregulation of the OmpF outer membrane protein in Escherichia coli. However, subsequent experiments with a micF deletion strain suggested that chromosomal micF RNA was not a key component in this process. We report here that micF RNA is essential for the reduction in OmpF levels in cells grown in media of low-to-intermediate levels of osmolarity. Under these conditions, the amount of OmpF was reduced up to 60%… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

2
39
0

Year Published

1995
1995
2018
2018

Publication Types

Select...
10

Relationship

0
10

Authors

Journals

citations
Cited by 50 publications
(41 citation statements)
references
References 48 publications
2
39
0
Order By: Relevance
“…In contrast to that of nearly all other osmotically regulated systems in E. coli, the osmotic control of s occurs at the posttranscriptional level (to our knowledge, the only other posttranscriptional osmoregulation is that of ompF by the micF antisense RNA during a shift from low to intermediate osmolarity [30]). In the case of s , increased translation and inhibition of s turnover contribute to osmotic induction (Fig.…”
Section: Discussionmentioning
confidence: 98%
“…In contrast to that of nearly all other osmotically regulated systems in E. coli, the osmotic control of s occurs at the posttranscriptional level (to our knowledge, the only other posttranscriptional osmoregulation is that of ompF by the micF antisense RNA during a shift from low to intermediate osmolarity [30]). In the case of s , increased translation and inhibition of s turnover contribute to osmotic induction (Fig.…”
Section: Discussionmentioning
confidence: 98%
“…Regulation in response to osmolarity is mediated by the OmpR-binding sites, integration host factor, and the micF gene (47,48,55), while the response to temperature is mediated by the micF gene (4). Previous studies have proposed that under low-osmolarity lake water at ambient temperature, OmpF is the major porin expressed; in contrast, under high-osmolarity animal intestine at 37Ā°C, OmpC is the predominant porin expressed (38,45).…”
Section: Discussionmentioning
confidence: 99%
“…However, this is based on experiments with sucrose rather than NaCl and not in the presence of glycine betaine, which may interfere with porin stoichiometry (34,35) together with other factors, such as glucose availability (31). In addition, small RNAs are involved posttranscriptionally with the regulation of these porins under osmotic stress, so their gene expression would not exactly correlate with levels of mature protein (36).…”
Section: Figmentioning
confidence: 99%