Literature DB >> 1541398

Structure of a gene encoding heat-shock protein HSP70 from the unicellular alga Chlamydomonas reinhardtii.

F W Müller1, G L Igloi, C F Beck.   

Abstract

The structure of a gene encoding a 70-kDa heat-shock protein (HSP70) from the unicellular alga, Chlamydomonas reinhardtii, is described. This gene shows a remarkable expression pattern, because it is inducible by light as well as by elevated temperature [von Gromoff et al., Mol. Cell. Biol. 9 (1989) 3911-3918]. As a first step in the investigation of trans-acting factors involved in environmentally controlled expression of this hsp70 gene, the nucleotide sequence of the entire gene, including its 5'- and 3'-flanking regions was determined. Although the deduced amino acid sequence exhibits a high degree of conservation to the HSP70 from higher plants, the C. reinhardtii gene has a unique structure among the members of the hsp70 gene family. While most hsp70 genes have only one or no intron, the coding region of the C. reinhardtii gene is interrupted by six introns. Besides putative TATA and CCAAT boxes, two heat-shock elements (HSE) were found in the promoter region, and a third HSE motif was located within the fourth intron. A computer search for regulatory cis-acting elements revealed a noted similarity of a 5'-upstream sequence motif to the G-box motif conserved in higher plants. A polyadenylation recognition sequence canonical for nuclear genes of C. reinhardtii is located downstream from the coding sequence.

Entities:  

Mesh:

Substances:

Year:  1992        PMID: 1541398     DOI: 10.1016/0378-1119(92)90684-h

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  27 in total

1.  Molecular cloning and expression of two HSP70 genes in the prawn, Macrobrachium rosenbergii.

Authors:  Jun Liu; Wei-Jun Yang; Xiao-Jing Zhu; Natalie K Karouna-Renier; Ranga K Rao
Journal:  Cell Stress Chaperones       Date:  2004       Impact factor: 3.667

2.  Proteomic analysis of a model unicellular green alga, Chlamydomonas reinhardtii, during short-term exposure to irradiance stress reveals significant down regulation of several heat-shock proteins.

Authors:  Bancha Mahong; Suttiruk Roytrakul; Narumon Phaonaklop; Janewit Wongratana; Kittisak Yokthongwattana
Journal:  Planta       Date:  2011-09-29       Impact factor: 4.116

3.  Characterization of a molecular chaperone present in the eukaryotic flagellum.

Authors:  Jessica Shapiro; Jessica Ingram; Karl A Johnson
Journal:  Eukaryot Cell       Date:  2005-09

4.  The Chlamydomonas genome reveals its secrets: chaperone genes and the potential roles of their gene products in the chloroplast.

Authors:  Michael Schroda
Journal:  Photosynth Res       Date:  2004       Impact factor: 3.573

5.  Phylogenetic analysis of the stress-70 protein family.

Authors:  S A Rensing; U G Maier
Journal:  J Mol Evol       Date:  1994-07       Impact factor: 2.395

6.  Transcription factor-dependent chromatin remodeling at heat shock and copper-responsive promoters in Chlamydomonas reinhardtii.

Authors:  Daniela Strenkert; Stefan Schmollinger; Frederik Sommer; Miriam Schulz-Raffelt; Michael Schroda
Journal:  Plant Cell       Date:  2011-06-24       Impact factor: 11.277

7.  Light-inducible gene HSP70B encodes a chloroplast-localized heat shock protein in Chlamydomonas reinhardtii.

Authors:  C Drzymalla; M Schroda; C F Beck
Journal:  Plant Mol Biol       Date:  1996-09       Impact factor: 4.076

Review 8.  Molecular chaperones and protein folding in plants.

Authors:  R S Boston; P V Viitanen; E Vierling
Journal:  Plant Mol Biol       Date:  1996-10       Impact factor: 4.076

9.  Expression of Hsp70 in the mud crab, Scylla paramamosain in response to bacterial, osmotic, and thermal stress.

Authors:  Ya'nan Yang; Haihui Ye; Huiyang Huang; Shaojing Li; Xueliang Liu; Xianglan Zeng; Jie Gong
Journal:  Cell Stress Chaperones       Date:  2013-01-17       Impact factor: 3.667

10.  Sequences controlling transcription of the Chlamydomonas reinhardtii beta 2-tubulin gene after deflagellation and during the cell cycle.

Authors:  J P Davies; A R Grossman
Journal:  Mol Cell Biol       Date:  1994-08       Impact factor: 4.272

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.