SASDCV5: Leishmania braziliensis p23A (Uncharacterized protein, Lbp23A)

基本情報

• 登録情報: データベース: SASBDB / ID: SASDCV5

試料

Leishmania braziliensis p23A

• Uncharacterized protein (protein), Lbp23A, Leishmania braziliensis

• 機能・相同性: Co-chaperone protein p23-like / CS domain / CS domain / CS domain profile. / HSP20-like chaperone / Hsp90 protein binding / CS domain-containing protein
• 生物種: Leishmania braziliensis (ブラジルリーシュマニア)
• 引用: ジャーナル: FEBS J / 年: 2015; タイトル: Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities.; 著者: Fernanda A H Batista / Glessler S Almeida / Thiago V Seraphim / Kelly P Silva / Silvane M F Murta / Leandro R S Barbosa / Júlio C Borges / ; 要旨: The small acidic protein called p23 acts as a co-chaperone for heat-shock protein of 90 kDa (Hsp90) during its ATPase cycle. p23 proteins inhibit Hsp90 ATPase activity and show intrinsic chaperone activity. A search for p23 in protozoa, especially trypanosomatids, led us to identify two putative proteins in the Leishmania braziliensis genome that share approximately 30% identity with each other and with the human p23. To understand the presence of two p23 isoforms in trypanosomatids, we obtained the recombinant p23 proteins of L. braziliensis (named Lbp23A and Lbp23B) and performed structural and functional studies. The recombinant proteins share similar solution structures; however, temperature- and chemical-induced unfolding experiments showed that Lbp23A is more stable than Lbp23B, suggesting that they may have different functions. Lbp23B prevented the temperature-induced aggregation of malic dehydrogenase more efficiently than did Lbp23A, whereas the two proteins had equivalent efficiencies with respect to preventing the temperature-induced aggregation of luciferase. Both proteins interacted with L. braziliensis Hsp90 (LbHsp90) and inhibited its ATPase activity, although their efficiencies differed. In vivo identification studies suggested that both proteins are present in L. braziliensis cells grown under different conditions, although Lbp23B may undergo post-translation modifications. Interaction studies indicated that both Lbp23 proteins interact with LbHsp90. Taken together, our data suggest that the two protozoa p23 isoforms act similarly when regulating Hsp90 function. However, they also have some differences, indicating that the L. braziliensis Hsp90 machine has features providing an opportunity for novel forms of selective inhibition of protozoan Hsp90.

登録者

• Júlio Borges (Instituto de Química de São Carlos, São Carlos - SP - Brasil)

モデル

• モデル #1322: ; タイプ: dummy / ソフトウェア: (5.0) / 対称性: P1 / カイ2乗値: 4.818025; Omokage検索でこの集合体の類似形状データを探す (詳細)

試料

• 試料: 名称: Leishmania braziliensis p23A / 試料濃度: 1.00-4.00
• バッファ: 名称: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol / pH: 8

要素 #705

名称: Lbp23A / タイプ: protein / 記述: Uncharacterized protein / 分子量: 22.09 / 分子数: 1 / 由来: Leishmania braziliensis / 参照: UniProt: A4HNB5
配列:

GSHMSHLPIK WAERKDRVFI TVEAMTASDV HVTFQEKTVS ISGYGVTAKG SEPHTLKGEL HLLKEIVPED STFKVLGVSI QICAMKKDQG YWNRLVEEPT KLTKSWLSAD WNLWKDEDDE AEEDAAASNF GGYGDMGGMD MGSMMGGMGG MGGMDMESMM ASMGKGAGGD SDDEEMADSE GEEQADDECE KSEEPAADIS DLNA

実験情報

• ビーム: 設備名称: Brazilian Synchrotron Light Laboratory SAXS2 Beamline; 地域: Campinas / 国: Brazil / 線源: X-ray synchrotron / 波長: 0.1488 Å / スペクトロメータ・検出器間距離: 1 mm
• 検出器: 名称: MAR 165 CCD

スキャン

タイトル: Leishmania braziliensis p23A / 測定日: 2012年3月26日 / 保管温度: 4 °C / セル温度: 20 °C / 照射時間: 300 sec. / 単位: 1/A /

	Min	Max
Q	0.0162	0.3346

距離分布関数 P(R)

ソフトウェア P(R): GNOM 4.5a / ポイント数: 248 /

	Min	Max
Q	0.01621	0.3346
P(R) point	1	248
R	0	130

結果

Experimental MW: 23 kDa / カーブのタイプ: single_conc

	P(R)	Guinier	P(R) error	Guinier error
前方散乱 I0	0.03181	0.031817	-	-
慣性半径, Rg	3.44 nm	3.33 nm	0.1	0.5

	Min	Max	Error
D	-	13	5
Guinier point	1	10	-