Molecular cloning of mouse glycolate oxidase. High evolutionary conservation and presence of an iron-responsive element-like sequence in the mRNA.

Kohler, Stefan A.; Menotti, Eric; Kühn, Lukas C.

doi:10.1016/s0021-9258(19)73113-5

Cited by 3 publications

(3 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…An IRE-like structure was also found upon in vitro selection in glycolate oxidase (HAO1) mRNA, but subsequently shown to be non-functional in 5 0 -UTR translational regulation. 38 Thus, defining physiologically relevant IREs requires both structural and functional criteria, among which evolutionary conservation helps to convince us of their pertinence.…”

Section: Ires In Various Mrnasmentioning

confidence: 99%

Iron regulatory proteins and their role in controlling iron metabolism

2015

Self Cite

View full text Add to dashboard Cite

Cellular iron homeostasis is regulated by post-transcriptional feedback mechanisms, which control the expression of proteins involved in iron uptake, release and storage. Two cytoplasmic proteins with mRNA-binding properties, iron regulatory proteins 1 and 2 (IRP1 and IRP2) play a central role in this regulation. Foremost, IRPs regulate ferritin H and ferritin L translation and thus iron storage, as well as transferrin receptor 1 (TfR1) mRNA stability, thereby adjusting receptor expression and iron uptake via receptor-mediated endocytosis of iron-loaded transferrin. In addition splice variants of iron transporters for import and export at the plasma-membrane, divalent metal transporter 1 (DMT1) and ferroportin are regulated by IRPs. These mechanisms have probably evolved to maintain the cytoplasmic labile iron pool (LIP) at an appropriate level. In certain tissues, the regulation exerted by IRPs influences iron homeostasis and utilization of the entire organism. In intestine, the control of ferritin expression limits intestinal iron absorption and, thus, whole body iron levels. In bone marrow, erythroid heme biosynthesis is coordinated with iron availability through IRP-mediated translational control of erythroid 5-aminolevulinate synthase mRNA. Moreover, the translational control of HIF2α mRNA in kidney by IRP1 coordinates erythropoietin synthesis with iron and oxygen supply. Besides IRPs, body iron absorption is negatively regulated by hepcidin. This peptide hormone, synthesized and secreted by the liver in response to high serum iron, downregulates ferroportin at the protein level and thereby limits iron absorption from the diet. Hepcidin will not be discussed in further detail here.

show abstract

Section: Ires In Various Mrnasmentioning

confidence: 99%

Iron regulatory proteins and their role in controlling iron metabolism

2015

Self Cite

View full text Add to dashboard Cite

show abstract

“…This is not surprising, considering that also HAOx sequences of higher eukaryotes were already successfully expressed in E. coli, ,,,, yet it shows that even when investigating unexplored sequence space of the HAOx family, expression of active enzymes in E. coli is not a limiting factor.…”

Section: Discussionmentioning

confidence: 99%

“…Expression of hitherto uncharacterized HAOx sequences showed that 41 out of 42 selected genes could be actively expressed in E. coli, indicating a good general expressability of HAOx family members. This is not surprising, considering that also HAOx sequences of higher eukaryotes were already successfully expressed in E. coli, 20,21,37,44,45 yet it shows that even when investigating unexplored sequence space of the HAOx family, expression of active enzymes in E. coli is not a limiting factor. An activity screening of these newly expressed HAOx members, using α-hydroxy acids of various chain lengths and structures, showed that L-lactate-specific enzymes are only found in one cluster, which was termed the "LOx cluster".…”

Section: ■ Discussionmentioning

confidence: 99%

Flavin Mononucleotide-Dependent l-Lactate Dehydrogenases: Expanding the Toolbox of Enzymes for l-Lactate Biosensors

et al. 2022

View full text Add to dashboard Cite

The development of L-lactate biosensors has been hampered in recent years by the lack of availability and knowledge about a wider range and diversity of L-lactate-oxidizing enzymes that can be used as bioelements in these sensors. For decades, L-lactate oxidase of Aerococcus viridans (AvLOx) has been used almost exclusively in the field of L-lactate biosensor development and has achieved somewhat like a monopoly status as a biocatalyst for these applications. Studies on other L-lactate-oxidizing enzymes are sparse and are often missing biochemical data. In this work, we made use of the vast amount of sequence information that is currently available on protein databases to investigate the naturally occurring diversity of L-lactate-utilizing enzymes of the flavin mononucleotide (FMN)-dependent α-hydroxy acid oxidoreductase (HAOx) family. We identified the HAOx sequence space specific for L-lactate oxidation and additionally discovered a not-yet described class of soluble and FMN-dependent L-lactate dehydrogenases, which are promising for the construction of second-generation biosensors or other biotechnological applications. Our work paves the way for new studies on α-hydroxy acid biosensors and proves that there is more to the HAOx family than AvLOx.

show abstract

AraPerox. A Database of Putative Arabidopsis Proteins from Plant Peroxisomes

et al. 2004

View full text Add to dashboard Cite

To identify unknown proteins from plant peroxisomes, the Arabidopsis genome was screened for proteins with putative major or minor peroxisome targeting signals type 1 or 2 (PTS1 or PTS2), as defined previously (Reumann S [2004] Plant Physiol 135: 783-800). About 220 and 60 proteins were identified that carry a putative PTS1 or PTS2, respectively. To further support postulated targeting to peroxisomes, several prediction programs were applied and the putative targeting domains analyzed for properties conserved in peroxisomal proteins and for PTS conservation in homologous plant expressed sequence tags. The majority of proteins with a major PTS and medium to high overall probability of peroxisomal targeting represent novel nonhypothetical proteins and include several enzymes involved in b-oxidation of unsaturated fatty acids and branched amino acids, and 2-hydroxy acid oxidases with a predicted function in fatty acid a-oxidation, as well as NADP-dependent dehydrogenases and reductases. In addition, large protein families with many putative peroxisomal isoforms were recognized, including acyl-activating enzymes, GDSL lipases, and small thioesterases. Several proteins are homologous to prokaryotic enzymes of a novel aerobic hybrid degradation pathway for aromatic compounds and proposed to be involved in peroxisomal biosynthesis of plant hormones like jasmonic acid, auxin, and salicylic acid. Putative regulatory proteins of plant peroxisomes include protein kinases, small heat shock proteins, and proteases. The information on subcellular targeting prediction, homology, and in silico expression analysis for these Arabidopsis proteins has been compiled in the public database AraPerox to accelerate discovery and experimental investigation of novel metabolic and regulatory pathways of plant peroxisomes.

show abstract

Molecular cloning of mouse glycolate oxidase. High evolutionary conservation and presence of an iron-responsive element-like sequence in the mRNA.

Cited by 3 publications

References 0 publications

Iron regulatory proteins and their role in controlling iron metabolism

Iron regulatory proteins and their role in controlling iron metabolism

Flavin Mononucleotide-Dependent l-Lactate Dehydrogenases: Expanding the Toolbox of Enzymes for l-Lactate Biosensors

AraPerox. A Database of Putative Arabidopsis Proteins from Plant Peroxisomes

Contact Info

Product

Resources

About