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Journal of Experimental Botany 2007 58(15-16):4373-4386; doi:10.1093/jxb/erm304
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© The Author [2008]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

RESEARCH PAPER

Localization and domain characterization of Arabidopsis golgin candidates

Maita Latijnhouwers1 *, Trudi Gillespie1 {dagger}, Petra Boevink1, Verena Kriechbaumer2 {ddagger}, Chris Hawes2,§ and Claudine M. Carvalho2 ¶

1Plant Pathology Programme, Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, UK
2School of Life Sciences, Oxford Brookes University, Headington, Oxford OX3 BP, UK

§ To whom correspondence should be addressed: chawes{at}brookes.ac.uk

Golgins are large coiled-coil proteins that play a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus. Six Arabidopsis proteins with the structural characteristics of golgins were isolated and shown to locate to Golgi stacks when fused to GFP. Two of these golgin candidates (GC1 and GC2) possess C-terminal transmembrane (TM) domains with similarity to the TM domain of human golgin-84. The C-termini of two others (GC3/GDAP1 and GC4) contain conserved GRAB and GA1 domains that are also found in yeast Rud3p and human GMAP210. GC5 shares similarity with yeast Sgm1p and human TMF and GC6 with yeast Uso1p and human p115. When fused to GFP, the C-terminal domains of AtCASP and GC1 to GC6 localized to the Golgi, showing that they contain Golgi localization motifs. The N-termini, on the other hand, label the cytosol or nucleus. Immuno-gold labelling and co-expression with the cis Golgi Q-SNARE Memb11 resulted in a more detailed picture of the sub-Golgi location of some of these putative golgins. Using two independent assays it is further demonstrated that the interaction between GC5, the TMF homologue, and the Rab6 homologues is conserved in plants.

Key words: Arabidopsis, AtGRIP, AtCASP, GDAP1, Golgi, golgin, Rab

* Present address: Department of Mathematics and Natural Sciences, University of Stavanger, Stavanger, 4036, Norway.

{dagger} Present address: IMPACT Confocal Microscope Facility, School of Biomedical Sciences, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK.

{ddagger} Present address: Faculty of Health and Wellbeing, Sheffield Hallam University, Howard Street, Sheffield S1 1WB, UK.

Present address: Federal University of Viçosa, BIOAGRO, Viçosa – MG, 36571 000, Brazil.

Received 20 September 2007; Revised 30 October 2007 Accepted 31 October 2007


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