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H, 13C, and 15N Backbone assignments of the human brain and acute leukemia cytoplasmic (BAALC) protein Andras Lang1   · Amit Kumar1 · Jan Jirschitzka2   · Frank Bordusa3 · Oliver Ohlenschläger1   · Christoph Wiedemann3  Received: 18 February 2020 / Accepted: 26 March 2020 © The Author(s) 2020

Abstract The brain and acute leukemia cytoplasmic (BAALC; UniProt entry Q8WXS3) is a 180-residue-long human protein having six known isoforms. BAALC is expressed in either hematopoietic or neuroectodermal cells and its specific function is still to be revealed. However, as a presumably membrane-anchored protein at the cytoplasmic side it is speculated that BAALC exerts its function at the postsynaptic densities of certain neurons and might play a role in developing cytogenetically normal acute myeloid leukemia (CN-AML) when it is highly overexpressed by myeloid or lymphoid progenitor cells. In order to better understand the physiological role of BAALC and to provide the basis for a further molecular characterization of BAALC, we report here the 1H, 13C, and 15N resonance assignments for the backbone nuclei of its longest hematopoietic isoform (isoform 1). In addition, we present a 1HN and 15NH chemical shift comparison of BAALC with its shortest, neuroectodermal isoform (isoform 6) which shows only minor changes in the 1H and 15N chemical shifts. Keywords  Resonance assignments · Heteronuclear NMR · Brain and acute leukemia cytoplasmic protein (BAALC) · Intrinsically disordered protein (IDP) · Neuroectodermal and hematopoietic cell function

Biological context The brain and acute leukemia cytoplasmic (BAALC; UniProt entry Q8WXS3) is a human protein of 180 amino acids. Eight alternatively spliced transcripts of BAALC were detected and five of them are described to form stable isoforms (isoform 1–3, 5 and 6) (Tanner et al. 2001). The remaining three splice variants encode the same predicted 80-amino-acid protein (isoform 4). These isoforms are expressed in cells of hematopoietic or neuroectodermal origin. The respective gene is located on chromosome 8q22.3 and is highly conserved in mammals and rodents (Fig. 1) but * Christoph Wiedemann [email protected]‑halle.de 1



Leibniz Institute on Aging – Fritz Lipmann Institute, Beutenbergstr. 11, 07745 Jena, Germany

2



Department of Chemistry, Institute of Biochemistry, University of Cologne, Zülpicher Str. 47, 50674 Cologne, Germany

3

Institute of Biochemistry and Biotechnology, Charles Tanford Protein Center, Martin-Luther-University Halle-Wittenberg, Kurt‑Mothes‑Str. 3a, 06120 Halle, Germany



absent in lower organisms (e.g. Caenorhabditis, Drosophila). Currently, the function of BAALC is not fully characterized, but studies indicate a high clinical significance in pathological processes from several leukemias [Acute Lymphoblastic Leukemia (Kuhnl et al. 2010) and Acute Myeloid Leukemia (Baldus et al. 2003b; Bienz et al. 2005; Marcucci et al. 2005) to trisomy 8/Warkany syndrome 2 (Hemsing et al. 2019)]. In bone marrow, the BAALC gene was shown

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