Backbone and side-chain resonance assignments ( 1 H, 15 N and 13 C) of the ubiquitin homology domain of mouse BAG-1
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ARTICLE
Backbone and side-chain resonance assignments (1H, 15N and 13C) of the ubiquitin homology domain of mouse BAG-1 Hsiao-Wen Huang • Chin Yu
Received: 29 April 2012 / Accepted: 7 August 2012 Ó Springer Science+Business Media B.V. 2012
Abstract BAG-1, an important regulatory protein associates with several signaling molecules and is capable of suppressing apoptosis. A 97-amino acid segment that includes the ubiquitin homology domain of mouse BAG-1 interacts with the cytoplasmic tail domain of proHB-EGF, and this interaction is likely to have functional significance. Here we report the backbone and side-chain resonance assignments for this 97-amino acid segment of mouse BAG-1. The assignment data has been deposited in the BMRB database under the accession number 18416. Keywords Ubiquitin homology domain Mouse BAG-1 Resonance assignment
Biological context The BAG (BCL2-associated athanogene)-family proteins (BAG-1, BAG-2, BAG-3, BAG-4, BAG-5) all contain a conserved region near their C termini (the BAG domain) that binds to Hsc70/Hsp70 and a central region that binds to Bcl-2, but they differ widely in their N-terminal domains. These proteins act as anti-apoptotic factor by inhibiting the chaperone activity of HSP70/HSC70 and increasing the anti-cell death function of BCL2 (Takayama
et al. 1999). The BAG-family proteins have been described to be involved in different cell processes linked to cell survival and were also found at high levels in several types of tumor cell lines (Batistatou et al. 2006; Clemo et al. 2008). BAG-1 (BCL2-associated athanogene 1) contains a unique ubiquitin homology (UBH) domain at the N terminus which enables interaction between BAG-1 and proteasome. The BAG-1’s ability to govern proteasomal degradation of certain proteins has been reported (Tsukahara and Maru 2010). However, the membrane form of the growth factor, HB-EGF, was demonstrated as a new binding partner of mouse BAG-1. The ubiquitin homology domain of mouse BAG-1 (residues 1-97) interacts with the 24-amino acid proHB-EGF cytoplasmic tail (Lin et al. 2001). We would like to study the interaction of BAG-1 with proHB-EGF at molecular level to understand more detail. The NMR structure of human BAG-1 (UBH) has been deposited on PDB (1 WXV). As the less sequence similarity between human and mouse BAG-1 in their ubiquitin homology domain (Fig. 1), understanding the structure of mouse BAG-1(UBH) is necessary. Here we report near complete sequence specific 1H, 13C and 15N assignments of mouse BAG-1 (UBH).
Methods and experiments Electronic supplementary material The online version of this article (doi:10.1007/s12104-012-9417-7) contains supplementary material, which is available to authorized users. H.-W. Huang C. Yu (&) Department of Chemistry, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu 30013, Taiwan, ROC e-mail: [email protected] H.-W. Huang e-mail: [email protected]
Sample preparation The cDNA encoding the mouse BAG-1-UBH (97 amino acid residues) was amplified by the polymerase ch
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