Skip Navigation


Molecular Plant Advance Access originally published online on June 23, 2008
Molecular Plant 2008 1(4):634-644; doi:10.1093/mp/ssn018
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Supplementary Data
Right arrow All Versions of this Article:
1/4/634    most recent
ssn018v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Kondo, K.
Right arrow Articles by McClure, B.
Right arrow Search for Related Content
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2008. Published by the Molecular Plant Shanghai Editorial Office in association with Oxford University Press on behalf of CSPP and IPPE, SIBS, CAS.

New microsome-associated HT-family proteins from Nicotiana respond to pollination and define an HT/NOD-24 protein family

Katsuhiko Kondo and Bruce McClure*

Department of Biochemistry, Interdisciplinary Plant Group, and the Christopher S. Bond Life Sciences Center, University of Missouri, MI, USA

* To whom correspondence should be addressed: E-mail mcclureb{at}missouri.edu

HT-family proteins have been identified in Nicotiana, Solanum, and Petunia. HT-B-type proteins are implicated in S-RNase-based self-incompatibility, but the functions of other family members are unknown. Screening for cDNA sequences with an expression pattern similar to HT-B in Nicotiana alata revealed a new group of small HT-family proteins, designated HT-M. HT-M proteins resemble HT-B in several respects: their pistil-specific expression pattern is indistinguishable from HT-B, they pellet with a microsome fraction, and their abundance decreases after pollination. Unlike HT-B, there is no S-specificity to this response, and RNAi experiments show that HT-M proteins are not necessary for self-incompatibility. Identification of a third group of pistil-specific HT-family proteins helps better define the characteristics of the family and allowed identification of putative new family members. By searching the databases with only the most conserved HT-family sequence elements, the signal sequence and cysteine motifs, we identified nodulin-24-like proteins and several small glycine-rich proteins as putative HT-family members. Like HT-M and HT-B, nodulin-24 is membrane associated. We propose that the conserved features in HT-family proteins are important for targeting or modification and refer to the broader family that includes both HT- and nodulin-24-like proteins as the HT/NOD-24-family.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J Exp BotHome page
A. R. Puerta, K. Ushijima, T. Koba, and H. Sassa
Identification and functional analysis of pistil self-incompatibility factor HT-B of Petunia
J. Exp. Bot., March 12, 2009; (2009) erp005v1.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
B. McClure
Darwin's foundation for investigating self-incompatibility and the progress toward a physiological model for S-RNase-based SI
J. Exp. Bot., March 1, 2009; 60(4): 1069 - 1081.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.