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Figure 9 | BMC Biochemistry

Figure 9

From: Importance of extended protease substrate recognition motifs in steering BNIP-2 cleavage by human and mouse granzymes B

Figure 9

Upstream translation initiation sites (uTIS) in the 5’ leader sequences of BNIP-2. A. Domain architecture and BCH domains of human and mouse BNIP-2 variants. In-frame translation products possessing a BCH domain were taken into account (i.e., four mouse (1–4) and two human (5–6) BNIP-2 variants). From top to bottom: 1. UniProtKB accession long mBNIP-2 (O54940) complemented with the 5′ leader from ENSMUSG00000011958; 2. Short mBNIP-2 [Trembl: Q91VL0]; 3. Long mBNIP-2 [Swiss-Prot: O54940]; 4. G5E8U9 (Trembl), 5. J3KN59 (Trembl) and 6. Human BNIP-2 [Swiss-Prot: Q12982]. Red bars are indicative for 5′ leader sequences whereas A, B and C annotations refer to putative alternative upstream translation initiation sites deduced from ribosome profiling analyses of a human (C) and mouse (A and B) cell line. B. Assessing the influence of 5′ leader sequences on BNIP-2 precursor patterns. The involvement of upstream translation initiation (uTIS) in the appearance of multiple precursor bands was investigated by transfecting BNIP-2 with or without its 5′ leader sequence in human HeLa and mouse NIH/3T3 cells. Black arrows indicate BNIP-2 precursors.

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