Cloning of a cDNA encoding bovine mitochondrial NADP+-specific isocitrate dehydrogenase and structural comparison with its isoenzymes from different species

Huh, Tae‐Lin; Ryu, Jin-Chang; Huh, Jae-Wook; Sung, Ha-Chin; Oh, Il-Ung; Song, Byoung Joon; Veech, R L

doi:10.1042/bj2920705

Cited by 38 publications

(33 citation statements)

References 35 publications

(39 reference statements)

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“…The icdk-2 cDNA had a length of 1569 bp and was predicted to encode a polypeptide of 416 amino acids, corresponding to about 45.5 kD. This finding fits well with determinations from other authors (Haselbeck and McAlister-Henn, 1991: yeast, 45 kD;Shorrosh and Dixon, 1992: alfalfa, 46 kD;Huh et al, 1993: bovine kidney, 46 kD). The 3' untranslated region of the cDNA includes the polyadenylation signal AATAAA (position 1378-1383).…”

Section: The Deduced Protein Sequence Of Icdh-1 From Potato Shows Sigsupporting

confidence: 80%

“…The overall sequence identity amounts to about 97% for tobacco (S. Gálvez, EMBL Data Library, accession No. X77944), to 90% for soybean (Udvardi et al, 1993) and alfalfa (Shorrosh and Dixon, 1992), to more than 65% for cattle (Huh et al, 1993), pig (Haselbeck et al, 1992), and yeast (Haselbeck and McAlister-Henn, 1991), and finally to 25% for Escherickiu coli (Thorsness and Koshland, 1987). Southern blot analysis of digested genomic DNA from potato probed with the complete icdh-2 cDNA fragment showed only a few bands (Fig.…”

Section: The Deduced Protein Sequence Of Icdh-1 From Potato Shows Sigmentioning

confidence: 99%

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Cloning and Expression Analysis of the Cytosolic NADP+-Dependent Isocitrate Dehydrogenase from Potato (Implications for Nitrogen Metabolism)

Fieuw¹,

Müller‐Röber²,

Gálvez³

et al. 1995

Plant Physiol.

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A full-length cDNA (icdb-7) encoding a cytosolic NADP+-dependent isocitrate dehydrogenase (ICDH-1) from potato (Solanum tuberosum L.) has been isolated. Analysis of the deduced protein sequence revealed considerable homologies with the corresponding proteins from other eukaryotes such as tobacco, alfalfa, soybean, cattle, pig, and yeast. The gene was transcribed in all tissues tested, with the highest amount of icdb-1 transcript being found in green tissues, i n flowers, and i n roots. In leaves, enzyme activities were dependent on the age, with fully mature leaves showing the highest level of RNA expression and enzyme activity. This observation may indicate that NADP+-dependent ICDH is not only involved in amino acid biosynthesis via the glutamine synthetase/glutamine oxoglutarate aminotransferase cycle but also in cycling, redistribution, and export of amino acids. The latter assumption has been strengthened by our finding of a preferential expression of NADP+-dependent ICDH in leaf veins. Under in vivo conditions, the expression pattern paralleled the enzyine activity, indicating coarse control on the RNA level. Experiments carried out with detached leaves revealed an influence of light, nitrate, and sucrose on icdh-1 transcript levels and i n some cases also on NADP+-dependent ICDH activity. I n darkness, nitrate or sucrose induced icdb-7 mRNA expression.Leaves kept under starvation conditions exhibited a decrease of their protein content, whereas icdh-1 expression and ICDH activity increased significantly.

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Section: The Deduced Protein Sequence Of Icdh-1 From Potato Shows Sigsupporting

confidence: 80%

Section: The Deduced Protein Sequence Of Icdh-1 From Potato Shows Sigmentioning

confidence: 99%

Cloning and Expression Analysis of the Cytosolic NADP+-Dependent Isocitrate Dehydrogenase from Potato (Implications for Nitrogen Metabolism)

Fieuw¹,

Müller‐Röber²,

Gálvez³

et al. 1995

Plant Physiol.

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“…Isocitrate NADP 2H Both isozymes have been purified from several mammals and their cDNA sequences were determined (Plaut et al 1983;Haselbeck et al 1992;Huh et al 1993;Jennings et al 1994;Loftus et al 1994;Yang et al 1996;Nekrutenko et al 1998). ICD1 and ICD2 are homodimers encoded in the nuclear genome (Loftus et al 1994).…”

mentioning

confidence: 99%

Localization of Cytosolic NADP-dependent Isocitrate Dehydrogenase in the Peroxisomes of Rat Liver Cells

Yoshihara

Hamamoto

Munakata

et al. 2001

J Histochem Cytochem.

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S U M M A R YTwo types of NADP-dependent isocitrate dehydrogenases (ICDs) have been reported: mitochondrial (ICD1) and cytosolic (ICD2). The C-terminal amino acid sequence of ICD2 has a tripeptide peroxisome targeting signal 1 sequence (PTS1). After differential centrifugation of the postnuclear fraction of rat liver homogenate, approximately 75% of ICD activity was found in the cytosolic fraction. To elucidate the true localization of ICD2 in rat hepatocytes, we analyzed the distribution of ICD activity and immunoreactivity in fractions isolated by Nycodenz gradient centrifugation and immunocytochemical localization of ICD2 antigenic sites in the cells. On Nycodenz gradient centrifugation of the light mitochondrial fraction, ICD2 activity was distributed in the fractions in which activity of catalase, a peroxisomal marker, was also detected, but a low level of activity was also detected in the fractions containing activity for succinate cytochrome C reductase (a mitochondrial marker) and acid phosphatase (a lysosomal marker). We have purified ICD2 from rat liver homogenate and raised a specific antibody to the enzyme. On SDS-PAGE, a single band with a molecular mass of 47 kD was observed, and on immunoblotting analysis of rat liver homogenate a single signal was detected. Double staining of catalase and ICD2 in rat liver revealed co-localization of both enzymes in the same cytoplasmic granules. Immunoelectron microscopy revealed gold particles with antigenic sites of ICD2 present mainly in peroxisomes. The results clearly indicated that ICD2 is a peroxisomal enzyme in rat hepatocytes. ICD2 has been regarded as a cytosolic enzyme, probably because the enzyme easily leaks out of peroxisomes during homogenization.

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“…Experiments using antibody-absorbing PVDF membranes showed that the anti-ICD1 peptide antibody could react with ICD1 to reduce the enzymatic activity in heart extract. Furthermore, Western blotting analysis showed that the anti-peptide antibody reacted with a single protein band with a molecular mass of 45 kD, which was considerably smaller than the unprocessed precursor form that had been predicted from DNA sequences so far: bovine, 50,824 (Huh et al 1993); human, 50,948 (Huh et al 1993); mouse, 58,749 (Yang et al 1996);pig, 47,526 (Haselbeck et al 1992); and yeast, 48,009 (Imajo et al 1997). These precursor forms of ICD1 seem to be imported into mitochondria and the signal sequence is cut off to form the mature enzyme.…”

Section: Specificity Of Antibodymentioning

confidence: 99%

“…Both enzymes have been purified from various sources and their cDNA sequences determined (Macfarlane et al 1977;Haselbeck et al 1992;Huh et al 1993;Jennings et al 1994;Loftus et al 1994;Yang et al 1996;Nekrutenko et al 1998). ICD1 and ICD2 are homodimers encoded in the nuclear genome (Loftus et al 1994).…”

mentioning

confidence: 99%

Localization of a Mitochondrial Type of NADP-dependent Isocitrate Dehydrogenase in Kidney and Heart of Rat: An Immunocytochemical and Biochemical Study

Haraguchi

Mabuchi

Yokota

2003

J Histochem Cytochem.

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S U M M A R YWe studied the subcellular localization of the mitochondrial type of NADPdependent isocitrate dehydrogenase (ICD1) in rat was immunofluorescence and immunoelectron microscopy and by biochemical methods, including immunoblotting and Nycodenz gradient centrifugation. Antibodies against a 14-amino-acid peptide at the C-terminus of mouse ICD1 was prepared. Immunoblotting analysis of the Triton X-100 extract of heart and kidney showed that the antibodies developed a single band with molecular mass of 45 kD. ICD1 was highly expressed in heart, kidney, and brown fat but only a low level of ICD1 was expressed in other tissues, including liver. Immunofluorescence staining showed that ICD1 was present mainly in mitochondria and, to a much lesser extent, in nuclei. Low but significant levels of activity and antigen of ICD1 were found in nuclei isolated by equilibrium sedimentation. Immunoblotting analysis of subcellular fractions isolated by Nycodenz gradient centrifugation from rat liver revealed that ICD1 signals were exclusively distributed in mitochondrial fractions in which acyl-CoA dehydrogenase was present. Immunofluorescence staining and postembedding electron microscopy demonstrated that ICD1 was confined almost exclusively to mitochondria and nuclei of rat kidney and heart muscle. The results show that ICD1 is expressed in the nuclei in addition to the mitochondria of rat heart and kidney. In the nuclei, the enzyme is associated with heterochromatin. In kidney, ICD1 distributes differentially in the tubule segments.

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Cloning of a cDNA encoding bovine mitochondrial NADP+-specific isocitrate dehydrogenase and structural comparison with its isoenzymes from different species

Cited by 38 publications

References 35 publications

Cloning and Expression Analysis of the Cytosolic NADP+-Dependent Isocitrate Dehydrogenase from Potato (Implications for Nitrogen Metabolism)

Cloning and Expression Analysis of the Cytosolic NADP+-Dependent Isocitrate Dehydrogenase from Potato (Implications for Nitrogen Metabolism)

Localization of Cytosolic NADP-dependent Isocitrate Dehydrogenase in the Peroxisomes of Rat Liver Cells

Localization of a Mitochondrial Type of NADP-dependent Isocitrate Dehydrogenase in Kidney and Heart of Rat: An Immunocytochemical and Biochemical Study

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