Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic
We have cloned and sequenced a gene (spaN) from Streptococcus lactis ATCC 11454 which encodes the peptide precursor of the small protein antibiotic nisin. The encoded precursor is 57 amino acids long, with a 23-residue leader region and a 34-residue structural region. The structural region contains serines, threonines, and cysteines at exactly the positions required to give mature nisin by a series of post-translational modifications involving dehydration of serines and threonines to dehydro forms, and cross-linking with cysteine residues. S1 mapping revealed a 267-nucleotide transcript of the nisin gene that is expressed during vegetative growth and stationary phase. It has a half-life of 7-10 min. The absence of an identifiable promoter or rho-independent terminator and the detection of two different 5'-ends of the transcript suggested it is a processing product from a larger RNA. This may represent a polycistronic mRNA which may also encode proteins involved in processing the nisin precursor peptide. Open reading frames were found in regions flanking the nisin gene. The one downstream had a ribosome binding site and appeared to be transcribed by read-through from the nisin gene. The one upstream had significant homology to a putative transposase from the Escherichia coli IS2 insertion element. Comparison of gene sequence homologies between nisin and the other lanthionine antibiotics, subtilin and epidermin, indicated that they all evolved from a common ancestor. Corresponding leader peptide sequences showed mediocre amino acid homology, but nearly perfect hydropathic homologies, suggesting a common function. It is proposed that this function includes recognition signals or other information required for post-translational processing.
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
1988 |
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| Erschienen: |
1988 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:263 |
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| Enthalten in: |
The Journal of biological chemistry - 263(1988), 31 vom: 05. Nov., Seite 16260-6 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Buchman, G W [VerfasserIn] |
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| Themen: |
1414-45-5 |
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| Anmerkungen: |
Date Completed 02.12.1988 Date Revised 10.02.2021 published: Print GENBANK: J04057 Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM031227244 |
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| 041 | |a eng | ||
| 100 | 1 | |a Buchman, G W |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic |
| 264 | 1 | |c 1988 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
| 338 | |a Band |b nc |2 rdacarrier | ||
| 500 | |a Date Completed 02.12.1988 | ||
| 500 | |a Date Revised 10.02.2021 | ||
| 500 | |a published: Print | ||
| 500 | |a GENBANK: J04057 | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a We have cloned and sequenced a gene (spaN) from Streptococcus lactis ATCC 11454 which encodes the peptide precursor of the small protein antibiotic nisin. The encoded precursor is 57 amino acids long, with a 23-residue leader region and a 34-residue structural region. The structural region contains serines, threonines, and cysteines at exactly the positions required to give mature nisin by a series of post-translational modifications involving dehydration of serines and threonines to dehydro forms, and cross-linking with cysteine residues. S1 mapping revealed a 267-nucleotide transcript of the nisin gene that is expressed during vegetative growth and stationary phase. It has a half-life of 7-10 min. The absence of an identifiable promoter or rho-independent terminator and the detection of two different 5'-ends of the transcript suggested it is a processing product from a larger RNA. This may represent a polycistronic mRNA which may also encode proteins involved in processing the nisin precursor peptide. Open reading frames were found in regions flanking the nisin gene. The one downstream had a ribosome binding site and appeared to be transcribed by read-through from the nisin gene. The one upstream had significant homology to a putative transposase from the Escherichia coli IS2 insertion element. Comparison of gene sequence homologies between nisin and the other lanthionine antibiotics, subtilin and epidermin, indicated that they all evolved from a common ancestor. Corresponding leader peptide sequences showed mediocre amino acid homology, but nearly perfect hydropathic homologies, suggesting a common function. It is proposed that this function includes recognition signals or other information required for post-translational processing | ||
| 650 | 4 | |a Comparative Study | |
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, U.S. Gov't, P.H.S. | |
| 650 | 7 | |a Nisin |2 NLM | |
| 650 | 7 | |a 1414-45-5 |2 NLM | |
| 700 | 1 | |a Banerjee, S |e verfasserin |4 aut | |
| 700 | 1 | |a Hansen, J N |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t The Journal of biological chemistry |d 1945 |g 263(1988), 31 vom: 05. Nov., Seite 16260-6 |w (DE-627)NLM000004995 |x 1083-351X |7 nnns |
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