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FCAPTUVBY photometry for the mCPstars HD32966, HD35298, HD68292, HD93226, HD171247, HD217833, HD220147, and HD223358 Abstract
We present differential Strömgren
uvbyobservations from the Four College Automated Photometric Telescope (FCAPT) in Washington Camp, AZ of eight magnetic Chemically Peculiar (mCP) stars: HD 32966, HD 35298, HD 68292, HD 93226, HD 171247, HD 217833, HD 220147, and HD 223358. We use multiple period‐finding algorithms and incorporate data from the ESA Hipparcos catalogue to study the amplitudes, periods, and asymmetries in the light curves. No previous FCAPT data have been published for HD 68292. For the seven other stars, these studies substantially extend the analyses of published FCAPT datasets.
RIP9 complexes associate with C‐to‐U RNAediting activity, PPRs, RIPs, OZ1, ORRM1 and ISE2 Summary
The mitochondrial and chloroplast
mRNAs of the majority of land plants are modified through cytidine to uridine (C‐to‐U) RNAediting. Previously, forward and reverse genetic screens demonstrated a requirement for pentatricopeptide repeat ( PPR) proteins for RNAediting. Moreover, chloroplast editing factors OZ1, RIP2, RIP9 and ORRM1 were identified in co‐immunoprecipitation (co‐IP) experiments, albeit the minimal complex sufficient for editing activity was never deduced. The current study focuses on isolated, intact complexes that are capable of editing distinct sites. Peak editing activity for four sites was discovered in size‐exclusion chromatography (SEC) fractions ≥ 670 kDa, while fractions estimated to be approximately 413 kDa exhibited the greatest ability to convert a substrate containing the editing site rps14C80. RNAcontent peaked in the ≥ 670 kDa fraction. Treatment of active chloroplast extracts with RNase A abolished the relationship of editing activity with high‐ MWfractions, suggesting a structural RNAcomponent in native complexes. By immunoblotting, RIP9, OTP86, OZ1 and ORRM1 were shown to be present in active gel filtration fractions, though OZ1 and ORRM1 were mainly found in low‐ MWinactive fractions. Active editing factor complexes were affinity‐purified using anti‐ RIP9 antibodies, and orthologs to putative Arabidopsis thaliana RNAediting factor PPRproteins, RIP2, RIP9, RIP1, OZ1, ORRM1 and ISE2 were identified via mass spectrometry. Westernmore »