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In chloroplasts, much of this regulation occurs at the post\u2010transcriptional level, but the proteins responsible are largely unknown. To discover proteins that impact <jats:italic>psbA<\/jats:italic> expression, we identified proteins that associate with maize <jats:italic>psbA<\/jats:italic> mRNA by: (i) formaldehyde cross\u2010linking of leaf tissue followed by antisense oligonucleotide affinity capture of <jats:italic>psbA<\/jats:italic> mRNA; and (ii) co\u2010immunoprecipitation with HCF173, a <jats:italic>psbA<\/jats:italic> translational activator that is known to bind <jats:italic>psbA<\/jats:italic> mRNA. The S1 domain protein SRRP1 and two RNA Recognition Motif (RRM) domain proteins, CP33C and CP33B, were enriched with both approaches. Orthologous proteins were also among the enriched protein set in a previous study in Arabidopsis that employed a designer RNA\u2010binding protein as a <jats:italic>psbA <\/jats:italic>RNA affinity tag. We show here that CP33B is bound to <jats:italic>psbA<\/jats:italic> mRNA <jats:italic>in vivo,<\/jats:italic> as was shown previously for CP33C and SRRP1. Immunoblot, pulse labeling, and ribosome profiling analyses of mutants lacking CP33B and\/or CP33C detected some decreases in D1 protein levels under some conditions, but no change in <jats:italic>psbA<\/jats:italic> RNA abundance or translation. However, analogous experiments showed that SRRP1 represses <jats:italic>psbA<\/jats:italic> ribosome association in the dark, represses <jats:italic>ycf1<\/jats:italic> ribosome association, and promotes accumulation of <jats:italic>ndhC<\/jats:italic> mRNA. As SRRP1 is known to harbor RNA chaperone activity, we postulate that SRRP1 mediates these effects by modulating RNA structures. The uncharacterized proteins that emerged from our analyses provide a resource for the discovery of proteins that impact the expression of <jats:italic>psbA<\/jats:italic> and other chloroplast genes.<\/jats:p>","DOI":"10.1111\/tpj.14629","type":"journal-article","created":{"date-parts":[[2019,12,3]],"date-time":"2019-12-03T03:33:56Z","timestamp":1575344036000},"page":"369-382","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["Exploring the proteome associated with the mRNA encoding the D1 reaction center protein of Photosystem II in plant chloroplasts"],"prefix":"10.1111","volume":"102","author":[{"given":"Kenneth P.","family":"Watkins","sequence":"first","affiliation":[{"name":"Institute of Molecular Biology University of Oregon Eugene OR 97403 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rosalind","family":"Williams\u2010Carrier","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biology University of Oregon Eugene OR 97403 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Prakitchai","family":"Chotewutmontri","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biology University of Oregon Eugene OR 97403 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Giulia","family":"Friso","sequence":"additional","affiliation":[{"name":"Section of Plant Biology School of Integrative Plant Sciences Cornell University Ithaca NY 14853 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marlene","family":"Teubner","sequence":"additional","affiliation":[{"name":"Institute of Biology Department of Life Sciences Humboldt University Berlin 10115 Berlin Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Susan","family":"Belcher","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biology University of Oregon Eugene OR 97403 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hannes","family":"Ruwe","sequence":"additional","affiliation":[{"name":"Institute of Biology Department of Life Sciences Humboldt University Berlin 10115 Berlin Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christian","family":"Schmitz\u2010Linneweber","sequence":"additional","affiliation":[{"name":"Institute of Biology Department of Life Sciences Humboldt University Berlin 10115 Berlin Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Klaas J.","family":"van Wijk","sequence":"additional","affiliation":[{"name":"Section of Plant Biology School of Integrative Plant Sciences Cornell University Ithaca NY 14853 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3049-2838","authenticated-orcid":false,"given":"Alice","family":"Barkan","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biology University of Oregon Eugene OR 97403 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2020,1,16]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/26.10.2265"},{"key":"e_1_2_9_3_1","doi-asserted-by":"publisher","DOI":"10.1104\/pp.110.171231"},{"key":"e_1_2_9_4_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.1001482"},{"key":"e_1_2_9_5_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1006106"},{"key":"e_1_2_9_6_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1007555"},{"key":"e_1_2_9_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2015.03.025"},{"key":"e_1_2_9_8_1","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1991.tb04974.x"},{"key":"e_1_2_9_9_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.7992056"},{"key":"e_1_2_9_10_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.1001731"},{"key":"e_1_2_9_11_1","doi-asserted-by":"publisher","DOI":"10.1104\/pp.109.152694"},{"key":"e_1_2_9_12_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0707851104"},{"key":"e_1_2_9_13_1","first-page":"295","article-title":"RNA processing and decay in plastids. 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