5 years ago

SIP1, a novel SOS2 interaction protein, is involved in salt-stress tolerance in Arabidopsis

A novel salt overly-sensitive 2 (SOS2) interaction protein was identified by yeast two hybrid (Y2H) library and was referred to as SOS2 interaction protein 1 (SIP1). SIP1 belongs to a plant-specific protein family, which contains a conserved domain that corresponds to a putative N-acetyltransferase. The members of this family are tolerant to heavy metals and oxidative stress. Here, SIP1 was identified as a salt-responsive gene. The sos2×sip1-1 double mutant was more sensitive than the sos2 single mutant upon salt stress, whereas the overexpression of SIP1 gene enhanced the plant salt tolerance, suggesting that SIP1 was involved in plant salt tolerance. We also found that SIP1 increasingly accumulated in response to salt stress, and this accumulation was inhibited in the sos2 mutant background. This finding suggests that the function of SIP1 upon salt stress was dependent on SOS2 protein. Further investigation suggested that SIP1 improved Arabidopsis tolerance to salt stress by reducing the ROS accumulation. Taken together, these findings reveal a novel function of SIP1 in adjusting Arabidopsis adaptation to salt stress.

Publisher URL: www.sciencedirect.com/science

DOI: S098194281830024X

You might also like
Discover & Discuss Important Research

Keeping up-to-date with research can feel impossible, with papers being published faster than you'll ever be able to read them. That's where Researcher comes in: we're simplifying discovery and making important discussions happen. With over 19,000 sources, including peer-reviewed journals, preprints, blogs, universities, podcasts and Live events across 10 research areas, you'll never miss what's important to you. It's like social media, but better. Oh, and we should mention - it's free.

  • Download from Google Play
  • Download from App Store
  • Download from AppInChina

Researcher displays publicly available abstracts and doesn’t host any full article content. If the content is open access, we will direct clicks from the abstracts to the publisher website and display the PDF copy on our platform. Clicks to view the full text will be directed to the publisher website, where only users with subscriptions or access through their institution are able to view the full article.