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Phosphoglycerylethanolamine Posttranslational Modification of Plant Eukaryotic Elongation Factor 1alpha 1

Wendy D. Ransom, Pao-Chi Lao, Douglas A. Gage, and Wendy F. Boss*

Botany Department, North Carolina State University, Raleigh, North Carolina 27695-7612 (W.D.R., W.F.B.); Department of Environmental and Occupational Health, National Cheng Kung Medical College, Tainan 70428, Taiwan, Republic of China (P.-C.L.); and Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824 (D.A.G.)

Eukaryotic elongation factor 1alpha (eEF-1A) is a multifunctional protein. There are three known posttranslational modifications of eEF-1A that could potentially affect its function. Except for phosphorylation, the other posttranslational modifications have not been demonstrated in plants. Using matrix-assisted laser desorption/ionization-mass spectrometry and peptide mass mapping, we show that carrot (Daucus carota L.) eEF-1A contains a phosphoglycerylethanolamine (PGE) posttranslational modification. eEF-1A was the only protein labeled with [14C]ethanolamine in carrot cells and was the predominant ethanolamine-labeled protein in Arabidopsis seedlings and tobacco (Nicotiana tabacum L.) cell cultures. In vivo-labeling studies using [3H]glycerol, [32P]Pi, [14C]myristic acid, and [14C]linoleic acid indicated that the entire phospholipid phosphatidylethanolamine is covalently attached to the protein. The PGE lipid modification did not affect the partitioning of eEF-1A in Triton X-114 or its actin-binding activity in in vitro assays. Our in vitro data indicate that this newly characterized posttranslational modification alone does not affect the function of eEF-1A. Therefore, the PGE lipid modification may work in combination with other posttranslational modifications to affect the distribution and the function of eEF-1A within the cell.

1   This research was supported by the National Science Foundation (grant no. MCB-9604285 to W.F.B.) and by a Patricia Roberts Harris fellowship to W.D.R. Acquisition of mass spectral data at Michigan State University-National Institutes of Health (NIH) Mass Spectrometry Facility was supported in part by the NIH (grant no. RR00480).
*   Corresponding author; e-mail wendy_boss{at}ncsu.edu; fax 1-919-515-3436.

Plant Physiol. (1998) 117: 949-960
Copyright Clearance Center:   0032-0889/98/117/0949/12
© 1998 American Society of Plant Physiologists




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