This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Web of Science (36) Citing Articles via Google Scholar Google Scholar Articles by Werner-Washburne, M. Articles by Keegstra, K. Search for Related Content PubMed PubMed Citation Articles by Werner-Washburne, M. Articles by Keegstra, K. Agricola Articles by Werner-Washburne, M. Articles by Keegstra, K.

Articles

Analysis of Pea Chloroplast Inner and Outer Envelope Membrane Proteins by Two-Dimensional Gel Electrophoresis and Their Comparison with Stromal Proteins ¹

Department of Botany, University of Wisconsin, Madison, Wisconsin 53706

Analysis of inner and outer pea (Pisum sativum var. Laxtons Progress No. 9) chloroplast envelope membranes by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that, although the two membranes have distinct polypeptide compositions, there are several comigrating polypeptides in the two membrane fractions. To determine whether these comigrating polypeptides were identical by criteria other than molecular weight, the membrane proteins were analyzed by two-dimensional gel electrophoresis. The results demonstrated that an 86-kilodalton band found in both membranes represents at least two different polypeptides, one an outer membrane protein and the other an inner membrane protein. Several other polypeptide bands found in both membranes appear to be of stromal origin. Two of these polypeptides were shown to be the large and small subunits of ribulose 1,5-bisphosphate carboxylase. The large subunit was identified by two-dimensional electrophoresis of envelope membranes to which stromal proteins were added. Additionally, the large and small subunits of ribulose 1,5-bisphosphate carboxylase were immunologically identified using an electrophoretic transfer procedure coupled with an enzyme-linked immunosorbent assay. Various treatments, including sonication, resulted in no significant loss of the stromal polypeptides from the outer envelope membranes. Based on these results, it is suggested that the stromal proteins are not simply bound to the outer surface of the vesicles.

This article has been cited by other articles:

				J. Jouhet and J. C. Gray Interaction of Actin and the Chloroplast Protein Import Apparatus J. Biol. Chem., July 10, 2009; 284(28): 19132 - 19141. [Abstract] [Full Text] [PDF]

				F. Bouvier, N. Linka, J.-C. Isner, J. Mutterer, A. P.M. Weber, and B. Camara Arabidopsis SAMT1 Defines a Plastid Transporter Regulating Plastid Biogenesis and Plant Development PLANT CELL, November 1, 2006; 18(11): 3088 - 3105. [Abstract] [Full Text] [PDF]

				E. J. Summer and K. Cline Red Bell Pepper Chromoplasts Exhibit in Vitro Import Competency and Membrane Targeting of Passenger Proteins from the Thylakoidal Sec and Delta pH Pathways but Not the Chloroplast Signal Recognition Particle Pathway Plant Physiology, February 1, 1999; 119(2): 575 - 584. [Abstract] [Full Text]

				H.-m. Li and L.-J. Chen A Novel Chloroplastic Outer Membrane-targeting Signal That Functions at Both Termini of Passenger Polypeptides J. Biol. Chem., April 18, 1997; 272(16): 10968 - 10974. [Abstract] [Full Text] [PDF]

				L. Kourtz and K. Ko The Early Stage of Chloroplast Protein Import Involves Com70 J. Biol. Chem., January 31, 1997; 272(5): 2808 - 2813. [Abstract] [Full Text] [PDF]