Journals / Turkish Journal of Biology / 2011 / Cilt: 35 - Sayı: 4

Molecular cloning, characterization, and expression analysis of a gene encoding a Ran binding protein (RanBP) in Cucumis melo L.

Pages
387–397
Publication Date
2011-04-01
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

We show here for the first time that the CmRanBP gene expression was correlated with heat stress responses.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Ran binding proteins (RanBPs) are highly conserved members of the GTP-binding protein family that are involved in nuclear protein export between the nucleus and the cytoplasm.
📊
Key Findings & Data:The 778 basepair long melon, with a RanBP cDNA encoding consisting of 197 amino acids (22.2 kDa protein), was characterized (GenBank accession no: EU853459).
💡
Conclusion & Impact:We show here for the first time that the CmRanBP gene expression was correlated with heat stress responses.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Key words: Melon (Cucumis melo L.) · Ran binding protein (RanBP) · gene cloning

Abstract

Ran binding proteins (RanBPs) are highly conserved members of the GTP-binding protein family that are involved in nuclear protein export between the nucleus and the cytoplasm. In this study, a CmRanBP gene from a melon was isolated (Cucumis melo L.) using the RACE (rapid amplification of cDNA ends) method. The 778 basepair long melon, with a RanBP cDNA encoding consisting of 197 amino acids (22.2 kDa protein), was characterized (GenBank accession no: EU853459). The predicted amino acid sequence of CmRanBP was found to be 70% identical to VvRanBP, PtRanBP, and RcRanBP from Vitis vinifera, Populus trichocarpa, and Ricinus communis, respectively. Within the RanBD (Ran binding domain), 5 highly conserved motifs and 1 Ran binding motif were found in all members of the RanBP gene family from various plant species. Expression profiles of the CmRanBP gene in different tissues under high temperature stress were also investigated by semiquantitative RT-PCR. The CmRanBP gene was expressed in a similar manner in the roots, leaves, and stems at 25 °C as a control environment. However, when the temperature was raised to 38 °C and 40 °C, expression levels of the CmRanBP gene were significantly (P < 0.05) increased in the root, leaf, and stem tissues. We show here for the first time that the CmRanBP gene expression was correlated with heat stress responses.

Özet

Ran binding proteins (RanBPs) are highly conserved members of the GTP-binding protein family that are involved in nuclear protein export between the nucleus and the cytoplasm. In this study, a CmRanBP gene from a melon was isolated (Cucumis melo L.) using the RACE (rapid amplification of cDNA ends) method. The 778 basepair long melon, with a RanBP cDNA encoding consisting of 197 amino acids (22.2 kDa protein), was characterized (GenBank accession no: EU853459). The predicted amino acid sequence of CmRanBP was found to be 70% identical to VvRanBP, PtRanBP, and RcRanBP from Vitis vinifera, Populus trichocarpa, and Ricinus communis, respectively. Within the RanBD (Ran binding domain), 5 highly conserved motifs and 1 Ran binding motif were found in all members of the RanBP gene family from various plant species. Expression profiles of the CmRanBP gene in different tissues under high temperature stress were also investigated by semiquantitative RT-PCR. The CmRanBP gene was expressed in a similar manner in the roots, leaves, and stems at 25 °C as a control environment. However, when the temperature was raised to 38 °C and 40 °C, expression levels of the CmRanBP gene were significantly (P < 0.05) increased in the root, leaf, and stem tissues. We show here for the first time that the CmRanBP gene expression was correlated with heat stress responses.

🔖

Cite This Article

BALOĞLU, M. C., ZAKHAROV, F. N., ÖKTEM, H. A., YÜCEL, A. M. (2011). Molecular cloning, characterization, and expression analysis of a gene encoding a Ran binding protein (RanBP) in Cucumis melo L.. Turkish Journal of Biology, Cilt: 35 - Sayı: 4, 387–397. https://ajindex.com/articles/182502

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (13)

  1. Faostat Agriculture data (http://faostat.fao.org/default.aspx) 2. Kirkbride JH. Biosystematic monograph of the genus Cucumis (Cucurbitaceae). Parkway Publishers,
  2. Boone, North Carolina; 1993. 3. Garcia-Mas J, Monforte AJ, Arus P. Phylogenetic relationships among Cucumis species based on the ribosomal internal transcribed spacer sequence and microsatellite markers. Plant Syst Evol 248, 191-203, 2004. 4. Liu L, Kakihara F, Kato M. Characterization of six varieties of Cucumis melo L. based on morphological and physiological characters, including shelf-life of fruit. Euphytica 135, 305-313, 2004.
  3. Bourne HR, Sanders DA, McCormick F. Th e GTPase superfamily: conserved structure and molecular mechanism. Nature 349, 117-127, 1991. 6. Takai Y, Sasaki T, Matozaki T. Small GTP-Binding Proteins. Physiol Rev 81, 153-208, 2001. 7. Görlich D, Dabrowski M, Bischoff FR et al. A novel class of RanGtp binding proteins. J Cell Biol 138, 65-80, 1997.
  4. Mattaj IW, Englmeier L. Nucleocytoplasmic transport: the soluble phase. Annu Rev Biochem 67, 265-306, 1998. 9. Nigg EA. Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 386, 779-787, 1997.
  5. Ohno M, Fornerod M, Mattaj IW. Nucleocytoplasmic transport: the last 200 nanometers. Cell 92, 327-336, 1998.
  6. Carazo-Salas RE, Guarguaglini G, Gruss OJ et al. Generation of GTP-bound Ran by RCC1 is required for chromatin-induced mitotic spindle formation. Nature 400, 178-181, 1999.
  7. Kahana JA, Cleveland DW. Beyond nuclear transport. Ran- GTP as a determinant of spindle assembly. J Cell Biol 146, 1205-1210, 1999.
  8. Kalab P, Pu RT, Dasso M. Th e Ran GTPase regulates mitotic spindle assembly. Curr Biol 9, 481-484, 1999.
  9. Tian B, Lin ZB, Ding Y et al. Cloning and characterization of a cDNA encoding Ran binding protein from wheat. Mitochondrial DNA 17, 136-142, 2006.
  10. Clarke PR, Zhang C. Ran GTPase: a master regulator of nuclear structure and function during the eukaryotic cell division cycle? Trends Cell Biol 11, 366-371, 2001.
  11. Haizel T, Merkle T, Pay A et al. Characterization of proteins that interact with the GTP-bound form of the regulatory GTPase Ran in Arabidopsis. Plant J 11, 93-103, 1997.
  12. Ach RA, Gruissem W. A small nuclear GTP-binding protein from tomato suppresses a Schizosaccharomyces pombe cell cycle mutant. Proc Natl Acad Sci 91, 5863-5867, 1994.
  13. Merkle T, Haizel T, Matsumoto T et al. Phenotype of the fi ssion yeast cell cycle regulatory mutant pim1-46 is suppressed by a tobacco cDNA encoding a small, Ran-like GTP-binding