Plant-Specific Protein MCD1 Determines the Site of Chloroplast Division in Concert with Bacteria-Derived MinD

نویسندگان

  • Hiromitsu Nakanishi
  • Kenji Suzuki
  • Yukihiro Kabeya
  • Shin-ya Miyagishima
چکیده

Chloroplasts evolved from a cyanobacterial endosymbiont, and chloroplast division requires the formation of an FtsZ division ring, which is descended from the cytokinetic machinery of cyanobacteria. As in bacteria, the positioning of the chloroplast FtsZ ring is regulated by the proteins MinD and MinE. However, chloroplast division also involves mechanisms invented by the eukaryotic host cell. Here we show that a plant-specific protein MULTIPLE CHLOROPLAST DIVISION SITE 1 (MCD1) regulates FtsZ ring positioning in Arabidopsis thaliana chloroplasts. Our analyses show that both MCD1 and MinD are required for chloroplast division, localizing at the division sites and punctate structures dispersed on the inner envelope. MinD overexpression inhibited FtsZ ring formation whereas MCD1 overexpression did not. Localization studies suggest that MCD1 is required for MinD localization to regulate FtsZ ring formation. Furthermore, the interaction between MCD1 and MinD in yeast two-hybrid assays suggests that MCD1 recruits MinD by direct interaction. These results point out differences in the MinD localization mechanism between chloroplasts and bacterial model systems and suggest that the plant cell evolved a component to modulate the cyanobacteria-derived Min system so as to regulate chloroplast FtsZ ring positioning.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

A homologue of the bacterial cell division site-determining factor MinD mediates placement of the chloroplast division apparatus

BACKGROUND Chloroplast division in plant cells occurs by binary fission, yielding two daughter plastids of equal size. Previously, we reported that two Arabidopsis homologues of FtsZ, a bacterial protein that forms a cytokinetic ring during cell division, are essential for plastid division in plants, and may be involved in the formation of plastid-dividing rings on both the stromal and cytosoli...

متن کامل

The Chloroplast Min System Functions Differentially in Two Specific Nongreen Plastids in Arabidopsis thaliana

The nongreen plastids, such as etioplasts, chromoplasts, etc., as well as chloroplasts, are all derived from proplastids in the meristem. To date, the Min system members in plants have been identified as regulators of FtsZ-ring placement, which are essential for the symmetrical division of chloroplasts. However, the regulation of FtsZ-ring placement in nongreen plastids is poorly understood. In...

متن کامل

Interdependency of formation and localisation of the Min complex controls symmetric plastid division.

Plastid division represents a fundamental biological process essential for plant development; however, the molecular basis of symmetric plastid division is unclear. AtMinE1 plays a pivotal role in selection of the plastid division site in concert with AtMinD1. AtMinE1 localises to discrete foci in chloroplasts and interacts with AtMinD1, which shows a similar localisation pattern. Here, we inve...

متن کامل

A plant-specific dynamin-related protein forms a ring at the chloroplast division site.

Chloroplasts have retained the bacterial FtsZ for division, whereas mitochondria lack FtsZ except in some lower eukaryotes. Instead, mitochondrial division involves a dynamin-related protein, suggesting that chloroplasts retained the bacterial division system, whereas a dynamin-based system replaced the bacterial system in mitochondria during evolution. In this study, we identified a novel plan...

متن کامل

Further evaluation of the localization and functionality of hemagglutinin epitope- and fluorescent protein-tagged AtMinD1 in Arabidopsis thaliana.

Symmetric chloroplast division requires a prokaryote-derived division regulator protein MinD, whose subchloroplastic localization remains to be completely established. We investigated the localization and functionality of AtMinD1 (Arabidopsis thaliana MinD) fused with a dual hemagglutinin epitope (dHA) or a yellow fluorescent protein (YFP). AtMinD1-dHA, which successfully complemented the arc11...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Current Biology

دوره 19  شماره 

صفحات  -

تاریخ انتشار 2009