Physical map location of the peptide methionine sulfoxide reductase gene on the Escherichia coli chromosome

Rahman, M A; Moskovitz, Jackob; Strassman, J; Weissbach, Herbert; Brot, Nathan

doi:10.1128/jb.176.5.1548-1549.1994

Cited by 5 publications

(3 citation statements)

References 6 publications

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“…To our knowledge, this is the first time that an MsrA gene has been found to be located near to a GST gene. An MsrA gene has been located previously on the E. coli chromosome between the cysQ gene and that coding for a pyrophosphatase [37]. RNA blot analysis indicated that the MsrA gene from O. anthropi, like the GST gene, appears to be monocistronically transcribed, and the transcript level increased during growth of the bacteria in the presence of phenolic compounds.…”

Section: Discussionmentioning

confidence: 99%

Bacterial peptide methionine sulphoxide reductase: co-induction with glutathione S-transferase during chemical stress conditions

Tamburro¹,

Allocati

Masulli

et al. 2001

Biochemical Journal

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Peptide methionine sulphoxide reductase (MsrA; EC 1.8.4.6) is a ubiquitous enzyme catalysing the reduction of methionine sulphoxide to methionine in proteins, while the glutathione S-transferases (GSTs) are a major family of detoxification enzymes. A gene homologous to MsrA was identified in a chromosomal fragment from the bacterium Ochrobactrum anthropi, and this gene is located just downstream of a GST gene identified previously (OaGST) [Favaloro, Tamburro, Angelucci, De Luca, Melino, Di Ilio and Rotilio (1998) Biochem. J. 335, 573–579]. This raises the question of whether the products of these two genes may be involved in a common cellular protection function. To test this hypothesis, the hypothetical MsrA protein has been overexpressed in Escherichia coli as a functional 51kDa GST fusion protein. Following cleavage with thrombin and purification, the soluble 24kDa protein showed MsrA activity with N-acetylmethionine sulphoxide as substrate, as well as with other sulphoxide compounds. Therefore polyclonal antibodies were raised against the recombinant protein, and the modulation of MsrA in this bacterium, grown in the presence of different stimulants simulating several stress conditions, was investigated. The level of expression of MsrA was detected both by measuring the mRNA level and by immunoblotting experiments, in addition to measuring its catalytic activity. MsrA is a constitutive enzyme which is also inducible by chemical stress involving phenolic compounds such as phenol and 4-chlorophenol. Recently we reported that the GST of this bacterium, like MsrA, is only modulated by toxic chemical compounds [Favaloro, Tamburro, Trofino, Bologna, Rotilio and Heipieper (2000) Biochem. J. 346, 553–559]; therefore this is the first indication of a co-induction of the MsrA and GST enzymes during chemical stress.

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Section: Discussionmentioning

confidence: 99%

Bacterial peptide methionine sulphoxide reductase: co-induction with glutathione S-transferase during chemical stress conditions

Tamburro¹,

Allocati

Masulli

et al. 2001

Biochemical Journal

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“…It is interesting to note how this modus operandi of cloning on the basis of homology to a sequence obtained in (a) single episode(s) of purification, resulted in the unwanted narrowing of the field of investigation, leading to the discovery of Msr forms that subsequently proved to be only specific for the reduction of l ‐Met‐ S ‐(O). Furthermore, pMsr of E. coli , and the enzymes that were later purified, were named MsrA , well before the existence of another group of enzymes, those responsible for the reduction of l ‐Met‐ R ‐(O), that were called MsrB , was recognized.…”

Section: The Progresses: Cloning Of Msrs and Discovery Of Their Stmentioning

confidence: 99%

The discovery of methionine sulfoxide reductase enzymes: An historical account and future perspectives

2015

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L-Methionine (L-Met) is the only sulphur-containing proteinogenic amino acid together with cysteine. Its importance is highlighted by it being the initiator amino acid for protein synthesis in all known living organisms. L-Met, free or inserted into proteins, is sensitive to oxidation of its sulfide moiety, with formation of L-Met sulfoxide. The sulfoxide could not be inserted into proteins, and the oxidation of L-Met in proteins often leads to the loss of biological activity of the affected molecule. Key discoveries revealed the existence, in rats, of a metabolic pathway for the reduction of free L-Met sulfoxide and, later, in Escherichia coli, of the enzymatic reduction of L-Met sulfoxide inserted in proteins. Upon oxidation, the sulphur atom becomes a new stereogenic center, and two stable diastereoisomers of L-Met sulfoxide exist. A fundamental discovery revealed the existence of two unrelated families of enzymes, MsrA and MsrB, whose members display opposite stereospecificity of reduction for the two sulfoxides. The importance of Msrs is additionally emphasized by the discovery that one of the only 25 selenoproteins expressed in humans is a Msr. The milestones on the road that led to the discovery and characterization of this group of antioxidant enzymes are recounted in this review.

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“…With the development of genetic cloning technology, in the early 1990s, scientists successfully identified MsrA in bovines and humans that are homologous to the E. coli peptide L-Met-O reductase, and found that MsrA is able to reduce both free and protein-bound L-Met-O [ 13 , 14 , 15 ]. During the same time, an MsrA and Trx homologous protein in Neisseria gonorrhoeae called PilB was found to be enzymatically active toward both L-Met-O (R) and L-Met-O (S) [ 16 ].…”

Section: Introductionmentioning

confidence: 99%

The Function of Selenium in Central Nervous System: Lessons from MsrB1 Knockout Mouse Models

et al. 2021

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MsrB1 used to be named selenoprotein R, for it was first identified as a selenocysteine containing protein by searching for the selenocysteine insert sequence (SECIS) in the human genome. Later, it was found that MsrB1 is homologous to PilB in Neisseria gonorrhoeae, which is a methionine sulfoxide reductase (Msr), specifically reducing L-methionine sulfoxide (L-Met-O) in proteins. In humans and mice, four members constitute the Msr family, which are MsrA, MsrB1, MsrB2, and MsrB3. MsrA can reduce free or protein-containing L-Met-O (S), whereas MsrBs can only function on the L-Met-O (R) epimer in proteins. Though there are isomerases existent that could transfer L-Met-O (S) to L-Met-O (R) and vice-versa, the loss of Msr individually results in different phenotypes in mice models. These observations indicate that the function of one Msr cannot be totally complemented by another. Among the mammalian Msrs, MsrB1 is the only selenocysteine-containing protein, and we recently found that loss of MsrB1 perturbs the synaptic plasticity in mice, along with the astrogliosis in their brains. In this review, we summarized the effects resulting from Msr deficiency and the bioactivity of selenium in the central nervous system, especially those that we learned from the MsrB1 knockout mouse model. We hope it will be helpful in better understanding how the trace element selenium participates in the reduction of L-Met-O and becomes involved in neurobiology.

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Physical map location of the peptide methionine sulfoxide reductase gene on the Escherichia coli chromosome

Cited by 5 publications

References 6 publications

Bacterial peptide methionine sulphoxide reductase: co-induction with glutathione S-transferase during chemical stress conditions

Bacterial peptide methionine sulphoxide reductase: co-induction with glutathione S-transferase during chemical stress conditions

The discovery of methionine sulfoxide reductase enzymes: An historical account and future perspectives

The Function of Selenium in Central Nervous System: Lessons from MsrB1 Knockout Mouse Models

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