Plant-specific 4/1 polypeptide interacts with an endoplasmic reticulum protein related to human BAP31.

Publisher: Springer-Verlag [etc.] Country of Publication: Germany NLM ID: 1250576 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1432-2048 (Electronic) Linking ISSN: 00320935 NLM ISO Abbreviation: Planta Subsets: MEDLINE

Original Publication: Berlin, New York, Springer-Verlag [etc.]

Sequence Homology, Amino Acid*; Endoplasmic Reticulum/*metabolism ; Membrane Proteins/*metabolism ; Peptides/*metabolism ; Plant Proteins/*metabolism ; Nicotiana/*metabolism; Amino Acid Sequence ; Cell Membrane/metabolism ; Humans ; Kinetics ; Plant Epidermis/cytology ; Plant Proteins/chemistry ; Protein Binding ; Recombinant Fusion Proteins/metabolism ; Species Specificity ; Subcellular Fractions/metabolism ; Surface Plasmon Resonance ; Transcriptional Activation/genetics ; Two-Hybrid System Techniques

Main Conclusion: The plant-specific 4/1 protein interacts, both in yeast two-hybrid system and in vitro, and co-localizes in plant cells with plant BAP-like protein, the orthologue of human protein BAP31. In yeast two-hybrid system, we identified a number of Nicotiana benthamiana protein interactors of Nt-4/1, the protein known to affect systemic transport of potato spindle tuber viroid. For one of these interactors, an orthologue of human B-cell receptor-associated protein 31 (BAP31) termed plant BAP-like protein (PBL), the ability to interact with Nt-4/1 was studied in greater detail. Analyses of purified proteins expressed in bacterial cells carried out in vitro with the surface plasmon resonance (SPR) spectroscopy revealed that the N. tabacum PBL (NtPBL) was able to interact with Nt-4/1 with high-affinity, and that their complex can form at physiologically relevant concentrations of both proteins. Subcellular localization studies of 4/1-GFP and NtPBL-mRFP transiently co-expressed in plant cells revealed the co-localization of the two fusion proteins in endoplasmic reticulum-associated bodies, suggesting their interaction in vivo. The N-terminal region of the Nt-4/1 protein was found to be required for the specific subcellular targeting of the protein, presumably due to a predicted amphipathic helix mediating association of the Nt-4/1 protein with cell membranes. Additionally, this region was found to contain a trans-activator domain responsible for the Nt-4/1 ability to activate transcription of a reporter gene in yeast.

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Keywords: BAP31*; Endoplasmic reticulum*; Plant protein 4/1*; Surface plasmon resonance*; Transient protein expression*; Yeast two-hybrid system*

0 (BCAP31 protein, human)
0 (Membrane Proteins)
0 (Peptides)
0 (Plant Proteins)
0 (Recombinant Fusion Proteins)

Date Created: 20161008 Date Completed: 20170424 Latest Revision: 20231213

20240628

10.1007/s00425-016-2601-8

27714454