DERA

Official Full Name

deoxyribose-phosphate aldolase

Organism

Homo sapiens

GeneID

51071

Background

Enables deoxyribose-phosphate aldolase activity. Involved in deoxyribonucleoside catabolic process. Located in nucleoplasm. [provided by Alliance of Genome Resources, Feb 2025]

Synonyms

DEOC; CGI-26;

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Detailed Information

Deoxyribose phosphate aldolase (EC 4.1.2.4) converts 2-deoxyribose-5-phosphate to glyceraldehyde-3-phosphate and acetaldehyde, and belongs to the core metabolism of living organisms. Deoxyribose phosphate aldolase activity has been previously shown to exist in human cells, but the protein responsible for this activity has never been formally identified.

Expression of DERA

In most cell lines, the level of deoxyribose phosphate aldolase activity correlated with the level of DERA expression. Indeed, high deoxyribose phosphate aldolase activity was found in Huh-7 cells, moderate activity in HepG2 and Jurkat cells, and low activity in HeLa and HEK293 cells. The only difference researchers noticed was in Caco-2 cells, which had lower deoxyribose phosphate aldolase activity despite higher DERA mRNA levels. This result is consistent with another finding that colon cancer LoVo cells do not show any detectable activity. The unexpectedly low deoxyribose phosphate aldolase activity observed in colon cancer cell lines may be due to specific post-translational events such as phosphorylation. Mutational studies of the bacterial enzyme have shown that mutation S239E decreases its activity. The corresponding position in human DERA, Thr292, was shown to be a possible target of Polo-like kinase 1 (PLK1), which is overexpressed in most cancer cells. Furthermore, it cannot be excluded that the amount of DERA protein may be regulated at the level of protein translation and/or degradation. Such mechanisms have recently been emphasized to explain the frequently observed lack of correlation between the cellular concentration of the protein and its mRNA abundance.

Function and Significance of DERA

DERA, which is expressed primarily in the lungs, liver, and colon, is the human deoxyribose phosphate aldolase. Among human cell lines, liver-derived Huh-7 cells have the highest DERA mRNA levels and deoxyribose phosphate aldolase activity. It was shown that DERA interacts with YBX1, a known stress granule component, and is recruited to stress granules following oxidative or mitochondrial stress. Furthermore, cells that down-regulated DERA expression using shRNA formed fewer stress granules and were more susceptible to apoptosis after clotrimazole stress, suggesting that DERA is important for stress granule formation. Furthermore, it was shown that DERA expression allowed cells in which mitochondrial ATP production was abolished to utilize extracellular deoxyinosine to maintain ATP levels.

Role of DERA in apoptosis

Endogenous DERA is present in both the cytoplasm and the nucleus, consistent with its role in deoxynucleotide metabolism. More surprisingly, DERA is recruited to the SG in response to energy starvation, oxidative stress, or mitochondrial stress.SG assembly is a major defense mechanism established by cells to avoid apoptosis and increase survival. For example, in erythrocytes that form spontaneous SGs, apoptosis increases by 60% when SG formation is blocked by downregulation of the core SG protein G3BP1. In addition to mRNA and core mRNA-binding proteins, SGs sequester pro-apoptotic proteins such as ROCK1, as well as ribosomal small subunits that prevent translational restart, and contain proteins that enable rapid cellular recovery after the end of stress and the disassembly of SGs, such as HNRNPA1, CASC3 or DDX3X. In addition, DERA may help cells recover energy after stress by catabolizing DR5P released by deoxyribonucleotide degradation.

References:

You ZY, Liu ZQ, Zheng YG, Shen YC. Characterization and application of a newly synthesized 2-deoxyribose-5-phosphate aldolase. J Ind Microbiol Biotechnol. 2013;40(1):29-39. doi:10.1007/s10295-012-1213-y
Pei X, Wang Q, Qiu X, Ying L, Tao J, Xie T. The fed-batch production of a thermophilic 2-deoxyribose-5-phosphate aldolase (DERA) in Escherichia coli by exponential feeding strategy control. Appl Biochem Biotechnol. 2010;162(5):1423-1434. doi:10.1007/s12010-010-8924-1
Salleron L, Magistrelli G, Mary C, Fischer N, Bairoch A, Lane L. DERA is the human deoxyribose phosphate aldolase and is involved in stress response. Biochim Biophys Acta. 2014;1843(12):2913-2925. doi:10.1016/j.bbamcr.2014.09.007

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