Special Issue "Protein-Protein Interactions"
A special issue of Biology (ISSN 2079-7737).
Deadline for manuscript submissions: closed (30 November 2014)
Manuscript Submission Information
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
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The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Type of Paper: Article
Title: A pull-down method for an intra-cross linked peptide with a cell-free translation system
Authors: Yutaro Tanemura, Yuki Mochizuki, Shigeyuki Kumachi, Naoto Nemoto
Affiliations: Graduate School of Science and Engineering, Saitama University, Saitama, Japan; E-Mail: firstname.lastname@example.org
Abstract: Constrained peptides are an attractive class as affinity regents or drug leads owing to their exhibit excellent binding properties. Many kinds of constrained peptides, such as cyclic peptides, have been found in nature or designed artificially by directed evolution. However, confirming binding properties of the constrained peptides can generally be troublesome because the synthesis of constrained peptides is more complicated in comparison with linear peptides. In this paper, we showed that biotinylated constrained peptides containing a disulfide bridge or a chemical cross-linking could be synthesized using a cell-free translation system and analyzed with a puromycin-linker in the manner of pull-down assay method.
Type of paper: Review
Title: Eukaryotic LYR proteins interact with ancient mitochondrial protein complexes
Author: Heike Angerer
Affiliation: Goethe University Frankfurt, Medical School, Institute of Biochemistry II, Structural Bioenergetics Group, Frankfurt am Main, Germany; E-Mail: Angerer@em.uni-frankfurt.de
Abstract: In eukaryotic cells mitochondria host ancient essential bioenergetic and biosynthetic pathways that are under nuclear control. LYR (leucine/tyrosine/arginine) motif proteins (LYRMs) of the Complex1_LYR-like superfamily interact with protein complexes of alpha-proteobacteria origin. Many LYR proteins function as extra subunits or novel assembly factors of the oxidative phosphorylation (OXPHOS) core complexes. Structural insights about complex I accessory subunits LYRM6 and LYRM3 have been provided by structural analyses of EM and X-ray structures of complex I from bovine and the yeast Yarrowia lipolytica, respectively. Both LYRMs anchor independently an acyl carrier protein (ACPM) to complex I. The function of this duplicated protein interaction of ACPM with respiratory complex I is still unknown. Analysis of protein-protein interaction screens, genetic analyses and predicted multi-domain LYRMs offer further clues on an interaction network of LYR proteins in mitochondria.
Title: KAP1 is a novel substrate for the arginine methyltransferase PRMT5
Authors: Roberta di Caprio, Michela Ciano, Giorgia Montano, Paola Costanzo and Elena Cesaro
Affiliations: Department of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, Italy; E-Mail: email@example.com
Abstract: KAP1, the transcriptional corepressor of Kruppel-associated box zinc finger proteins (KRAB-ZFPs), is subjected to multiple post-translational modifications that are involved in fine-tuning of its multiple biological functions.
We previously identified the protein arginine methyltransferase PRMT5 as a component of repression complex mediated by the KRAB-ZFP ZNF224. In this study, we show that KAP1 interacts with PRMT5 and is a novel substrate for PRMT5 methylation. Also, we present evidence that the methylation of KAP1 arginine residues regulate the KAP1-ZNF224 interaction, thus suggesting that this KAP1 post-transcriptional modification could actively contribute to the regulation of ZNF224-mediated repression.