Skip to main content
SpringerLink
Log in

Both chloroplastic and cytosolic phosphofructoaldolase isozymes are present in the pea leaf nucleus

  • Published:
Protoplasma Aims and scope Submit manuscript

Summary.

In higher plants, fructose bisphosphate aldolase (EC 4.1.2.13) occurs in chloroplast, cytosol, and nucleus. Immunocytolocalization experiments with isozyme-directed antibodies indicate that both chloroplastic and cytosolic aldolase isoforms are present in the pea (Pisum sativum L.) leaf nucleus.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

anti-CpALD109–128:

antibody raised against a peptide corresponding to residues 109 through 128 of pea chloroplastic phosphofructoaldolase

anti-CpALDCterm:

antibody raised against a 20-residue peptide corresponding to the C terminus of the pea chloroplastic phosphofructoaldolase isozyme

anti-CyALD:

antibody raised against a peptide corresponding to residues 114 through 133 of pea cytosolic phosphofructoaldolase

SDS:

sodium dodecyl sulfate

References

  • JB Anderson AA Carol VK Brown LE Anderson (2003) ArticleTitleA quantitative method for assessing co-localization in immuno-labeled thin section electron micrographs. J Struct Biol 143 95–106 Occurrence Handle10.1016/S1047-8477(03)00138-2 Occurrence Handle1:CAS:528:DC%2BD3sXntVGltbg%3D Occurrence Handle12972346

    Article  CAS  PubMed  Google Scholar 

  • LE Anderson AA Carol (2004) ArticleTitleSeven enzymes of carbon metabolism, including three Calvin cycle isozymes, are present in the secondary cell wall thickenings of the developing xylem tracheary elements in pea leaves. Int J Plant Sci 165 243–256 Occurrence Handle10.1086/381918 Occurrence Handle1:CAS:528:DC%2BD2cXlvFCis70%3D

    Article  CAS  Google Scholar 

  • – Heinrikson RL, Noyes C (1975) Chloroplast and cytoplasmic enzymes: subunit structure of pea leaf aldolases. Arch Biochem Biophys 169: 262–268

    Google Scholar 

  • – Wang X, Gibbons JT (1995a) Three enzymes of carbon metabolism, or their antigenic analogs, in pea nuclei. Plant Physiol 108: 659–667

    Google Scholar 

  • – Goldhaber-Gordon IM, Li D, Tang X-Y, Xiang M, Prakash N (1995b) Enzyme-enzyme interaction in the chloroplast: glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase. Planta 196: 245–255

    Google Scholar 

  • – Yousefzai R, Ringenberg MR, Carol AA (2004a) Both chloroplastic and cytosolic fructose bisphosphatase isozymes are present in the pea leaf nucleus. Plant Sci 166: 721–730

    Google Scholar 

  • – Bryant JA, Carol AA (2004b) Both chloroplastic and cytosolic phosphoglycerate kinase isozymes are present in the pea leaf nucleus. Protoplasma 223: 103–110

    Google Scholar 

  • – Ringenberg MR, Carol AA (2004c) Cytosolic glyceraldehyde-3-P dehydrogenase and the B subunit of the chloroplast enzyme are present in the pea leaf nucleus. Protoplasma 223: 33–43

    Google Scholar 

  • SL Harmer JB Hogenesch M Straume H-S Chang B Han T Zhu X Wang JA Kreps SA Kay (2000) ArticleTitleOrchestrated transcription of key pathways in Arabidopsis by the circadian clock. Science 290 2110–2113 Occurrence Handle10.1126/science.290.5499.2110 Occurrence Handle1:CAS:528:DC%2BD3cXptVyisrw%3D Occurrence Handle11118138

    Article  CAS  PubMed  Google Scholar 

  • R Hayama T Izawa K Shimamoto (2002) ArticleTitleIsolation of rice genes possibly involved in the photoperiodic control of flowering by a fluorescent differential display method. Plant Cell Physiol 43 494–504 Occurrence Handle10.1093/pcp/pcf059 Occurrence Handle1:CAS:528:DC%2BD38XktFWgt78%3D Occurrence Handle12040096

    Article  CAS  PubMed  Google Scholar 

  • S Jacobshagen JR Whetstine JM Boling (2001) ArticleTitleMany but not all genes in Chlamydomonas reinhardtii are regulated by the circadian clock. Plant Biol 3 592–597 Occurrence Handle10.1055/s-2001-19370 Occurrence Handle1:CAS:528:DC%2BD38XnsVyktQ%3D%3D

    Article  CAS  Google Scholar 

  • A Kiri G Goldspink (2002) ArticleTitleRNA-protein interactions of the 3′ untranslated regions of myosin heavy chain transcripts. J Muscle Res Cell Motil 23 119–129 Occurrence Handle10.1023/A:1020211729728 Occurrence Handle1:CAS:528:DC%2BD38XntFSguro%3D Occurrence Handle12416718

    Article  CAS  PubMed  Google Scholar 

  • JJ Marchalonis MK Adelman IF Robey SF Schluter AB Edmundson (2001) ArticleTitleExquisite specificity and peptide epitope recognition promiscuity, properties shared by antibodies from sharks to humans. J Mol Recognit 14 110–121 Occurrence Handle10.1002/jmr.527 Occurrence Handle1:CAS:528:DC%2BD3MXjtlGhtr8%3D Occurrence Handle11301481

    Article  CAS  PubMed  Google Scholar 

  • G Minaschek U Groschel-Stewart S Blum J Bereiter-Hahn (1992) ArticleTitleMicrocompartmentation of glycolytic enzymes in cultured cells. Eur J Cell Biol 58 418–428 Occurrence Handle1:CAS:528:DyaK38XmsVyqt7g%3D Occurrence Handle1330571

    CAS  PubMed  Google Scholar 

  • T Nakagawa Y Hirano A Inomata S Yokota K Miyachi M Kaneda M Umeda K Furukawa S Omata T Horigome (2003) ArticleTitleParticipation of a fusogenic protein, glyceraldehyde-3-phosphate dehydrogenase, in nuclear membrane assembly. J Biol Chem 278 20395–20404 Occurrence Handle10.1074/jbc.M210824200 Occurrence Handle1:CAS:528:DC%2BD3sXktVejsLg%3D Occurrence Handle12651855

    Article  CAS  PubMed  Google Scholar 

  • K Razdan RL Heinrikson H Zurcher-Neely PW Morris LE Anderson (1992) ArticleTitleChloroplast and cytoplasmic enzymes: isolation and sequencing of cDNAs coding for two distinct pea chloroplast aldolases. Arch Biochem Biophys 298 192–197 Occurrence Handle10.1016/0003-9861(92)90112-A Occurrence Handle1:CAS:528:DyaK3sXktVertbs%3D Occurrence Handle1524427

    Article  CAS  PubMed  Google Scholar 

  • NE Robinson AB Robinson (2001) ArticleTitleMolecular clocks. Proc Natl Acad Sci 98 944–949 Occurrence Handle1:CAS:528:DC%2BD3MXht1Sms74%3D Occurrence Handle11158575

    CAS  PubMed  Google Scholar 

  • Z Ronai R Robinson S Rutberg P Lazarus M Sardana (1992) ArticleTitleAldolase DNA interactions in a SEWA cell system. Biochim Biophys Acta 1130 20–28 Occurrence Handle1:CAS:528:DyaK38XhsV2htL0%3D Occurrence Handle1543745

    CAS  PubMed  Google Scholar 

  • DE Saez JC Slebe (2000) ArticleTitleSubcellular localization of aldolase B. J Cell Biochem 78 62–72 Occurrence Handle1:CAS:528:DC%2BD3cXksVGqtrg%3D Occurrence Handle10797566

    CAS  PubMed  Google Scholar 

  • W Satou H Tanimoto R Ukekawa M Fujii D Ayusawa (2004) ArticleTitleAmplification of nuclear aldolase A in mouse cell mutants resistant to Hoechst 33342. Biochem Biophys Res Commun 315 845–849 Occurrence Handle10.1016/j.bbrc.2004.01.142 Occurrence Handle1:CAS:528:DC%2BD2cXhsFWmt7w%3D Occurrence Handle14985089

    Article  CAS  PubMed  Google Scholar 

  • AJ Yañez HC Ludwig R Bertinat C Spichiger R Gatica G Berlien O Leon M Brito II Concha JC Slebe (2005) ArticleTitleDifferent involvement for aldolase isoenzymes in kidney glucose metabolism: aldolase B but not aldolase A colocalizes and forms a complex with FBPase. J Cell Physiol 202 743–753 Occurrence Handle15389646

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biological Sciences, University of Illinois-Chicago, Chicago, Illinois

    L. E. Anderson, M. R. Ringenberg, V. K. Brown & A. A. Carol

Authors
  1. L. E. Anderson
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. M. R. Ringenberg
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. V. K. Brown
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. A. A. Carol
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to L. E. Anderson.

Additional information

Correspondence and reprints: Department of Biological Sciences m/c 066, University of Illinois-Chicago, 845 West Taylor, Chicago, Illinois 60607-7060, U.S.A.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Anderson, L., Ringenberg, M., Brown, V. et al. Both chloroplastic and cytosolic phosphofructoaldolase isozymes are present in the pea leaf nucleus. Protoplasma 225, 235–242 (2005). https://doi.org/10.1007/s00709-005-0099-1

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00709-005-0099-1

Search

Navigation