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Biology subjects

Huber, E. M.

Publications and source records attributed to Huber, E. M..

2 recordsLinked to original sources

Identification and biosynthesis of xildivaline, a novel and widespread peptide deformylase inhibitor from Gammaproteobacteria

Xenorhabdus strains, Gram-negative bacteria pathogenic to insects and symbionts to nematodes of the genus Steinernema are prolific producers of various natural products. Here we describe the xisABCDE biosynthesis gene cluster from Xenorhabdus hominickii responsible for the production of xildivalines. These non-ribosomal peptide and polyketide hybrids act as peptide deformylase inhibitor (PDI) and occur also in other Gammaproteobacteria, especially Vibrio. Their structure and biosynthesis were fully elucidated despite their instability, highlighting a rare trans-methylation of their N-terminus. Subsequently, the structure of the responsible methyltransferase XisE and the peptide deformylase XisD, serving as resistance mechanism, were elucidated by X-ray crystallography, allowing insights into the function and the mode of action of this novel class of PDIs.

microbiology↗

Cooperative DNA base and shape recognition by the CCAAT-binding complex and its bZIP transcription factor HapX

The heterotrimeric CCAAT-binding complex (CBC) is a master regulator of transcription. It specifically recognizes the CCAAT-box, a fundamental eukaryotic promoter element. Certain fungi, like Aspergilli, encode a fourth CBC-subunit, HapX, to fine-tune expression of genes involved in iron metabolism. Although being a basic region leucine zipper with its own DNA recognition motif, HapX function strictly relies on the CBC. We here report two crystal structures of the CBC-HapX complex bound to DNA duplexes with distinct sequence and position of HapX sites. In either structure, a HapX dimer targets the nucleic acid downstream of the CCAAT-box and the leash-like N-terminus of the distal HapX subunit interacts with CBC and DNA. In vitro and in vivo analyses of HapX mutants support the structures, highlight the complex as an exceptional major and minor groove DNA binder, and enrich our understanding of the functional as well as structural plasticity of related complexes across species.

biochemistry↗