KOPRI Repository

Protein adaptation in polar environment: a comparative study of α-tubulin sequences in mesophilic and psychrophilic polar microalgae

Metadata Downloads
Title
Protein adaptation in polar environment: a comparative study of α-tubulin sequences in mesophilic and psychrophilic polar microalgae
Other Titles
극지미세조류와 비극지미세조류의 tubulin 염기서열비교를 통한 단백질의 저온적응 기작연구
Authors
Jung, Min Gui
Han, Jong Won
Kang, Sung-Ho
Choi, Han-Gu
Kim, Gwang Hoon
Kim, Sanghee
Kim, Min-Jung
Keywords
Protein adaptation; mesophilic microalgae; psychrophilic polar microalgae; α-tubulin
Issue Date
2011
Citation
Jung, Min Gui, et al. 2011. Protein adaptation in polar environment: a comparative study of α-tubulin sequences in mesophilic and psychrophilic polar microalgae. 한국조류학회. 한국조류학회. 2011.12.06~.
Abstract
Although microtubules usually disassemble at low temperature below 4℃ by disturbing polymerization of tubulin dimer, organisms living in a cold environment seem to overcome this limit by amino acid substitution of tubulin. We aimed to investigate whether amino acid substitution on tubulin occur commonly in polar microalgae and is responsible for promoting growth at freezing temperature at which non-cold adapted algae seldom grow and eventually die. The full-length cDNAs of α-tubulin from eight genera with 14 microalgal strains (ArF04, ArF08, ArF13, ArF24, ArF25, ArF26, ArF27, ArF28, ArF29, ArF32, AnF48, AnM08, AnM30, and AnM45) collected from the Arctic and the Antarctic were obtained by RACE and compared them with that of α-tubulin from mesophilic alga, Chlamydomonas reinhardtii. We found that the several amino acid substitutions occurred in most tubulins of polar microalgae. These substitutions were found in overlapped sites reported in previous work, presumably due to selective pressure of cold environment. Of the substituted sequences, the A295V region was conspicuous, which has reported that play an important role in the producing protofilament due to the increasing hydrophobicity. 10 out of 14 microalgal strains (72%) showed a substitution of alanine (A) to valine (V) in the 295th residue demonstrating that the substitution of A295V region is a largely conserved fe
URI
http://repository.kopri.re.kr/handle/201206/8466
Conference Name
한국조류학회
Conference Place
한국조류학회
Conference Date
2011.12.06~
Files in This Item
There are no files associated with this item.
General Conditions
      ROMEO Green
    Can archive pre-print and post-print or publisher's version/PDF
      ROMEO Blue
    Can archive post-print (ie final draft post-refereeing) or publisher's version/PDF
      ROMEO Yellow
    Can archive pre-print (ie pre-refereeing)
      ROMEO White
    Archiving not formally supported

    qrcode

    Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

    Browse