R
Roland Kellner
Researcher at University of Tübingen
Publications - 21
Citations - 1398
Roland Kellner is an academic researcher from University of Tübingen. The author has contributed to research in topics: Lantibiotics & Staphylococcus gallinarum. The author has an hindex of 12, co-authored 21 publications receiving 1365 citations.
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Journal ArticleDOI
Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings
Schnell Norbert,Karl-Dieter Entian,Ursula Schneider,Friedrich Götz,Hans Zähner,Roland Kellner,Günther Jung +6 more
TL;DR: It is proposed that the N-terminus (–30 to –1) plays a cooperative role during modification reactions and prevents toxicity of the mature epidermin to the producing strain before the antibiotic is cleaved off and secreted.
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Gallidermin: a new lanthionine-containing polypeptide antibiotic.
Roland Kellner,Günther Jung,Thomas Hörner,Hans Zähner,Schnell Norbert,Karl-Dieter Entian,Friedrich Götz +6 more
TL;DR: The isolation procedures for gallidermin included adsorption directly from the culture broth, ion-exchange chromatography of the amphiphilic and basic polypeptide followed by desalting, and final purification by reversed-phase HPLC, which involved mainly a combination of automated gas-phase sequencing, thermospray liquid chromatography/mass spectrometry and fast-atom-bombardment mass spectromaetry.
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Pep5, a new lantibiotic: structural gene isolation and prepeptide sequence.
Kaletta Cortina,Karl-Dieter Entian,Roland Kellner,Günther Jung,Michaela Reis,Hans-Georg Sahl +5 more
TL;DR: The present theory is that maturation of Pep5 involves (a) enzymic conversion of Thr, Ser and Cys into dehydrated amino acids and sulfide bridges, (b) membrane translocation and cleavage of the modified prepeptide, which proves that Pep5 is ribosomally synthesized.
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Structural gene isolation and prepeptide sequence of gallidermin, a new lanthionine containing antibiotic
TL;DR: The isolation of a new lantibiotic, gallidermin, has been isolated from Staphyloccus gallinarum and its structural gene is named gdmA, which codes for a 52 amino acid residue prepeptide, consisting of an alpha-helical leader sequence of hydrophilic character.