Cloning and characterization of genes involved in the biosynthesis of δ-aminolevulinic acid in Escherichia coli

Ikemi, Masahisa; Murakami, Katsuji; Hashimoto, Masamichi; Murooka, Yoshikatsu

doi:10.1016/0378-1119(92)90170-t

Cited by 26 publications

(8 citation statements)

References 15 publications

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“…We therefore digested LolB with a limited amount of V8 protease and obtained two peptide fragments. The N‐terminal sequences of these fragments coincided with partial sequences of HemM (Figure 4A), which has been suggested to be involved in the synthesis of 5‐aminolevulinic acid, an intermediate of porphyrin biosynthesis (Ikemi et al ., 1992).…”

Section: Resultsmentioning

confidence: 68%

“…The hemM gene has been suggested by genetic analysis to be involved in the synthesis of 5‐aminolevulinic acid (Ikemi et al ., 1992). It was later found that hemA , but not hemM , is involved directly in 5‐aminolevulinic acid synthesis (Chen et al ., 1994; Hungerer et al ., 1995), although co‐expression of the two genes caused more efficient synthesis of 5‐aminolevulinic acid (Chen et al ., 1994).…”

Section: Discussionmentioning

confidence: 99%

“…A λ phage clone, 247 (15A7), in the Kohara library (Kohara et al ., 1987) was used to clone the hemM ( lolB ) gene as reported previously (Ikemi et al ., 1992). Based on the reported nucleotide sequence around the hemM ( lolB ) gene (Post et al ., 1993), a 1.7 kb Nhe I– Hin dIII DNA fragment was isolated from the λ DNA.…”

Section: Methodsmentioning

confidence: 99%

“…Thus, two factors, LolA and LolB, functioning in the release and incorporation of lipoproteins, respectively, have now been characterized. LolB was found to be the product of hemM , which has been suggested to be important for 5‐aminolevulinic acid synthesis (Ikemi et al ., 1992). However, the results shown here indicate that this is highly unlikely.…”

Section: Introductionmentioning

confidence: 99%

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A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli

Matsuyama¹

1997

The EMBO Journal

192

211

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The Escherichia coli major outer membrane lipoprotein (Lpp) is released from the inner membrane into the periplasm as a complex with a carrier protein, LolA (p20), and is then specifically incorporated into the outer membrane. An outer membrane protein playing a critical role in Lpp incorporation was identified, and partial amino acid sequences of the protein, named LolB, were identical to those of HemM, which has been suggested to play a role in 5-aminolevulinic acid synthesis in the cytosol. In contrast to this suggested role, the deduced amino acid sequence of HemM implied that the gene encodes a novel outer membrane lipoprotein. Indeed, an antibody raised against highly purified LolB revealed its outer membrane localization, and inhibited in vitro Lpp incorporation into the outer membrane. Furthermore, LolB was found to be synthesized as a precursor with a signal sequence and then processed to a lipid-modified mature form. An E.coli strain possessing chromosomal hemM under the control of the lac promoter-operator required IPTG for growth, indicating that hemM (lolB) is an essential gene. Outer membrane prepared from LolB-depleted cells did not incorporate Lpp. When the Lpp-LolA complex was incubated with a water-soluble LolB derivative, Lpp was transferred from LolA to LolB. Based on these results, the outer membrane localization pathway for E.coli lipoprotein is discussed with respect to the functions of LolA and LolB.

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Section: Resultsmentioning

confidence: 68%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli

Matsuyama¹

1997

The EMBO Journal

192

211

View full text Add to dashboard Cite

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“…Using these conditions, we were interested to examine to what extent the metabolic strategy employed by E. coli (fermentation vs. respiration) impacts its interaction with the electrode. E. coli SHSP18 has a defective respiratory chain that can be restored by supplementation with ALA [24,25]. SHSP18 was only able to initiate a detection event for 5000 CFU at 13.8 h in the absence of ALA compared to 6.6 h when the defective respiratory chain was restored by supplementing the medium with 20 µg mL −1 ALA (Figure 4).…”

Section: Resultsmentioning

confidence: 99%

Parameter Selection for a Microvolume Electrochemical Escherichia coli Detector for Pairing with a Concentration Device

Han

Kannan

Hinks

et al. 2019

Sensors

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Waterborne infections are responsible for health problems worldwide and their prompt and sensitive detection in recreational and potable water is of great importance. Bacterial identification and enumeration in water samples ensures water is safe for its intended use. Culture-based methods can be time consuming and are usually performed offsite. There is a need to for automated and distributed at-source detectors for water quality monitoring. Herein we demonstrate a microvolume Escherichia coli (E. coli) detector based on a screen printed electrode (SPE) bioelectroanalytical system and explore to what extent performance can be improved by coupling it with a filtration device. To confidently benchmark detector performance, we applied a statistical assessment method to target optimal detection of a simulated concentrated sample. Our aim was to arrive at a holistic understanding of device performance and to demonstrate system improvements based on these insights. The best achievable detection time for a simulated 1 CFU mL−1 sample was 4.3 (±0.6) h assuming no loss of performance in the filtration step. The real filtered samples fell short of this, extending detection time to 16–18 h. The loss in performance is likely to arise from stress imposed by the filtration step which inhibited microbial growth rates.

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The common origins of the pigments of life?early steps of chlorophyll biosynthesis

Avissar

Moberg

1995

Photosynth Res

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The complex pathway of tetrapyrrole biosynthesis can be dissected into five sections: the pathways that produce 5-aminolevulinate (the C-4 and the C-5 pathways), the steps that transform ALA to uroporphyrinogen III, which are ubiquitous in the biosynthesis of all tetrapyrroles, and the three branches producing specialized end products. These end products include corrins and siroheme, chlorophylls and hemes and linear tetrapyrroles. These branches have been subjects of recent reviews. This review concentrates on the early steps leading up to uroporphyrinogen III formation which have been investigated intensively in recent years in animals, in plants, and in a wide range of bacteria.

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Cloning and characterization of genes involved in the biosynthesis of δ-aminolevulinic acid in Escherichia coli

Cited by 26 publications

References 15 publications

A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli

A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli

Parameter Selection for a Microvolume Electrochemical Escherichia coli Detector for Pairing with a Concentration Device

The common origins of the pigments of life?early steps of chlorophyll biosynthesis

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