دورية أكاديمية

[Conservative motif CMLD in silicic acid transport proteins of diatom algae].

التفاصيل البيبلوغرافية
العنوان: [Conservative motif CMLD in silicic acid transport proteins of diatom algae].
المؤلفون: Shcherbakova TA, Masiukova IuA, Safonova TA, Petrova DP, Vereshchagin AL, Minaeva TV, Adel'shin RV, Triboĭ TI, Stonik IV, Aĭzdaĭcher NA, Kozlov MV, Likhoshvaĭ EV, Grachev MA
المصدر: Molekuliarnaia biologiia [Mol Biol (Mosk)] 2005 Mar-Apr; Vol. 39 (2), pp. 303-16.
نوع المنشور: English Abstract; Journal Article
اللغة: Russian
بيانات الدورية: Publisher: Izdatelstvo Nauka Country of Publication: Russia (Federation) NLM ID: 0105454 Publication Model: Print Cited Medium: Print ISSN: 0026-8984 (Print) Linking ISSN: 00268984 NLM ISO Abbreviation: Mol Biol (Mosk) Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Moskva : Izdatelstvo Nauka
مواضيع طبية MeSH: Amino Acid Motifs*, Carrier Proteins/*chemistry , Diatoms/*metabolism , Silicic Acid/*metabolism, Amino Acid Sequence ; Base Sequence ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; DNA ; Diatoms/genetics ; Kinetics ; Molecular Sequence Data ; Sequence Homology, Amino Acid ; Sequence Homology, Nucleic Acid
مستخلص: Sequencing of fragments of genes coding for silicic acid transport (SIT) proteins of diatoms of evolutionary distant classes (centric Chaetoceros muelleri Lemmermann, pennate araphid Synedra acus Kützing, pennate raphid Phaeodactylum tricornutum Bohlin, and pennate with keeled raphe system Cylindrotheca fusiformis Reimann et Lewin), revealed the presence in these proteins of a conservative amino acid motif CMLD. Hydropathy profiles suggest that CMLD occupies a position between two transmembrane strands which do not contain lysine and arginine residues. The two strands are good candidates for the role of the channel along which transport of silicic acid occurs. CMLD is a rare motif. Diatoms are known to need Zn2+ for the incorporation of silica. Presumably, CMLD is the site of Zn2+ binding of SITs. We found that the growth of diatoms is inhibited by a negatively charged alkylating reagent 5-(2-iodoacetamidoethyl)aminonaphtalene-1-sulfonic acid which cannot penetrate through the cell membrane. Cysteine of CMLD can be a target of this reagent. Synthetic peptide NCMLDY forms a complex with Zn2+, as revealed by the fact that the ion considerably reduces the rate of alkylation of the peptide.
المشرفين على المادة: 0 (Carrier Proteins)
1343-98-2 (Silicic Acid)
9007-49-2 (DNA)
تواريخ الأحداث: Date Created: 20050429 Date Completed: 20050630 Latest Revision: 20061115
رمز التحديث: 20240628
PMID: 15856954
قاعدة البيانات: MEDLINE