HO1 Antibody

Heme oxygenase 1 (HO1) is a key enzyme in the biosynthesis of the chromophore in plant phytochrome photoreceptors. It catalyzes the opening of the heme ring, yielding the open-chain tetrapyrrole biliverdin IXα, along with the release of iron and carbon monoxide (CO). This enzyme exhibits a specific preference for producing the biliverdin IXα isomer. HO1 forms a complex with heme, is ferredoxin-dependent, and its activity is enhanced by ascorbate. It plays a significant role in salt acclimation signaling and may influence the plastid-to-nucleus signaling pathway by modulating tetrapyrrole synthesis. This plastid-to-nucleus signaling is crucial for the coordinated expression of nuclear and chloroplast genes encoding photosynthesis-related proteins.

Research Highlights on HO1 Function:

• HO1 negatively regulates drought signaling upstream of ABSCISIC ACID-INSENSITIVE4 (ABI4). (PMID: 26704641)
• HO1 enhances cadmium tolerance by reducing nitric oxide production and improving iron homeostasis. (PMID: 23974911)
• HO1 overexpression increases nitric oxide (NO) levels, while its knockdown reduces NO levels in plants. (PMID: 23620481)
• HO1 mutants exhibit increased salt sensitivity. (PMID: 23744476)
• Disruption of AtHBP5 binding to HO1 leads to oxidative stress. (PMID: 22991161)
• HO1 mutations cause UV-C hypersensitivity due to impaired carotenoid and flavonoid biosynthesis and downregulation of antioxidant defenses. (PMID: 22419743)
• HO1 and HY5 additively regulate the expression of light-regulated genes and the accumulation of chlorophyll and anthocyanin during early seedling development. (PMID: 22424472)
• HO1 plays a crucial role in salt acclimation. (PMID: 21205037)
• HO1 subfamily members (HY1, HO3, and HO4) are active monomeric heme oxygenases that convert heme to BV IXα using spinach ferredoxin as an electron donor. (PMID: 19860740)

KEGG: ath:AT2G26670

STRING: 3702.AT2G26670.1

UniGene: At.23645