DIFFERENTIAL PROTEOME ANALYSIS CHARACTERIZATION OF ARABIDOPSIS HETEROTRIMERIC Gα SUBUNIT MUTANT

CHRISTIAN LISI, ANA ROMINA FOX, JORGE MUSCHIETTI AND AGUSTINA MAZZELLA

Tucuman

Congreso; SAIB; 2009

&amp;amp;lt;!-- /* Style Definitions */ p.MsoNormal, li.MsoNormal, div.MsoNormal {mso-style-parent:""; margin:0in; margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:12.0pt; font-family:"Times New Roman"; mso-fareast-font-family:"Times New Roman"; mso-ansi-language:ES; mso-fareast-language:ES;} @page Section1 {size:8.5in 11.0in; margin:1.0in 1.25in 1.0in 1.25in; mso-header-margin:.5in; mso-footer-margin:.5in; mso-paper-source:0;} div.Section1 {page:Section1;} --&amp;amp;gt; In higher plants many classes of biotic and abiotic signals act through specific transduction mechanisms to coordinate plant development. Heterotrimeric G protein signaling is one of the most conserved mechanisms in eukaryotes. Arabidopsis thaliana possess only one gene encoding a unique α subunit protein: AtGPA1. The evidence revealed that GPA1 is a central molecule in transmitting hormone, light and other signals to different effectors molecules. GPA1 has been described as a positive modulator of cell proliferation and gpa1 mutant leaves display a particular morphology. GPA1 mediated functions have been well described however only a few downstream effectors have been identified.  Nowadays, proteomic is a powerful technique defining proteins that change in abundance, form, location and can be used to identify proteins involved in specific developmental or environmental changes. Here, we obtained the proteome profile of wild type and gpa1 mutant leaves with the proposed to find differentially expressed proteins. Two dimensional gel electrophoresis revealed seven protein spots that showed statistically significant changes (p< 0.05) between the two phenotypes. Five proteins were more abundant in wild type plants and only two proteins were more abundant in gpa1 mutants. Spot excision, trypsin digestion and peptide mass sequencing is being conducting to obtain protein identities.