{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T14:13:38Z","timestamp":1784124818855,"version":"3.55.0"},"reference-count":64,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2025,1,23]],"date-time":"2025-01-23T00:00:00Z","timestamp":1737590400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100008982","name":"National Science Foundation of Sri Lanka","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008982","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2025,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>Starch accumulation in plants provides carbon for nighttime use, for regrowth after periods of dormancy, and for times of stress. Both \u0251\u2010 and \u03b2\u2010amylases (AMYs and BAMs, respectively) catalyze starch hydrolysis, but their functional roles are unclear. Moreover, the presence of catalytically inactive amylases that show starch excess phenotypes when deleted presents questions on how starch degradation is regulated. Plants lacking one of these catalytically inactive \u03b2\u2010amylases, BAM9, have enhanced starch accumulation when combined with mutations in BAM1 and BAM3, the primary starch degrading BAMs in response to stress and at night, respectively. BAM9 has been reported to be transcriptionally induced by stress although the mechanism for BAM9 function is unclear. From yeast two\u2010hybrid experiments, we identified the plastid\u2010localized AMY3 as a potential interaction partner for BAM9. We found that BAM9 interacted with AMY3 in\u00a0vitro and that BAM9 enhances AMY3 activity about three\u2010fold. Modeling of the AMY3\u2010BAM9 complex predicted a previously undescribed alpha\u2013alpha hairpin in AMY3 that could serve as a potential interaction site. Additionally, AMY3 lacking the alpha\u2013alpha hairpin is unaffected by BAM9. Structural analysis of AMY3 showed that it can form a homodimer in solution and that BAM9 appears to replace one of the AMY3 monomers to form a heterodimer. The presence of both BAM9 and AMY3 in many vascular plant lineages, along with model\u2010based evidence that they heterodimerize, suggests that the interaction is conserved. Collectively these data suggest that BAM9 is a pseudoamylase that activates AMY3 in response to cellular stress, possibly facilitating stress recovery.<\/jats:p>","DOI":"10.1002\/prot.26803","type":"journal-article","created":{"date-parts":[[2025,1,23]],"date-time":"2025-01-23T06:59:31Z","timestamp":1737615571000},"page":"1189-1201","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["The Pseudoenzyme \u03b2\u2010Amylase9 From Arabidopsis Activates \u03b1\u2010Amylase3: A Possible Mechanism to Promote Stress\u2010Induced Starch Degradation"],"prefix":"10.1002","volume":"93","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4285-4341","authenticated-orcid":false,"given":"Christopher E.","family":"Berndsen","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry James Madison University  Harrisonburg Virginia USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amanda 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