Abstract:
:The major anionic phospholipids of Escherichia coli, phosphatidylglycerol (PG) and cardiolipin (CL), have been considered to be indispensable for essential cellular functions, such as the initiation of DNA replication and translocation of proteins across the cytoplasmic membrane. However, we successfully constructed a null pgsA mutant of E. coli that had undetectable levels of PG and CL if the major outer membrane lipoprotein was deficient, clearly indicating that these anionic phospholipids are not indispensable. In the null mutant, we observed the accumulation of phosphatidic acid, an acidic biosynthetic precursor. This suggests a functionally substitutable nature of these anionic phospholipids and allows us to formulate a dual role model for the physiological roles of the anionic phospholipids in E. coli. The anionic phospholipids may play dual roles in E. coli as (i) substrates for head group-specific enzyme reactions, albeit the viability of null PG mutants indicates that the products of head group-specific reactions are not essential; and (ii) those that are replaceable, partly or entirely, by other phospholipids bearing net negative charges, because of their rather loose head group specificity. These two aspects of the physiological roles of anionic phospholipids are discussed with special reference to the phospholipids of other bacteria and eukaryotic organelles.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Matsumoto Kdoi
10.1046/j.1365-2958.2001.02320.xsubject
Has Abstractpub_date
2001-03-01 00:00:00pages
1427-33issue
6eissn
0950-382Xissn
1365-2958pii
mmi2320journal_volume
39pub_type
杂志文章,评审abstract::Whereas in Bacillus subtilis, a general stress response stimulon under the control of a single sigma factor (SigB) is induced by different physiological and environmental stresses (heat, salt or ethanol shock), in Streptomyces coelicolor, these environmental stresses induce independent sets of proteins, and its genome...
journal_title:Molecular microbiology
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abstract::The diffusible factor synthase XanB2, originally identified in Xanthomonas campestris pv. campestris (Xcc), is highly conserved across a wide range of bacterial species, but its substrate and catalytic mechanism have not yet been investigated. Here, we show that XanB2 is a unique bifunctional chorismatase that hydroly...
journal_title:Molecular microbiology
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journal_title:Molecular microbiology
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journal_title:Molecular microbiology
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更新日期:1996-07-01 00:00:00
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pub_type: 杂志文章
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更新日期:2014-01-01 00:00:00
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pub_type: 杂志文章,评审
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journal_title:Molecular microbiology
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