The DHC1b (DHC2) isoform of cytoplasmic dynein is required for flagellar assembly.
AuthorsPazour GJ, Dickert BL, Witman GB
JournalJ Cell Biol
PubMed ID9971742
'Dyneins are microtubule-based molecular motors involved in many different types of cell movement. Most dynein heavy chains (DHCs) clearly group into cytoplasmic or axonemal isoforms. However, DHC1b has been enigmatic. To learn more about this isoform, we isolated Chlamydomonas cDNA clones encoding a portion of DHC1b, and used these clones ... More
The maize homologue of the cell cycle checkpoint protein MAD2 reveals kinetochore substructure and contrasting mitotic and meiotic localization patterns.
AuthorsYu HG, Muszynski MG, Kelly Dawe R
JournalJ Cell Biol
PubMed ID10225945
'We have identified a maize homologue of yeast MAD2, an essential component in the spindle checkpoint pathway that ensures metaphase is complete before anaphase begins. Combined immunolocalization of MAD2 and a recently cloned maize CENPC homologue indicates that MAD2 localizes to an outer domain of the prometaphase kinetochore. MAD2 staining ... More
Thr-161 Phosphorylation of Monomeric Cdc2. REGULATION BY PROTEIN PHOSPHATASE 2C IN XENOPUS OOCYTES.
'Fully grown Xenopus oocyte is arrested at prophase I of meiosis. Re-entry into meiosis depends on the activation of MPF (M-phase promoting factor or cyclin B.Cdc2 complex), triggered by progesterone. The prophase-arrested oocyte contains a store of Cdc2. Most of the protein is present as a monomer whereas a minor ... More
Differential and Independent Roles of a 32 Homolog (RpoH) and an HrcA Repressor in the Heat Shock Response of Agrobacterium tumefaciens
AuthorsKenji Nakahigashi,1, Eliora Z. Ron,2 Hideki Yanagi,1 and Takashi Yura1,*
JournalJ Bacteriol
PubMed ID10601208
'The heat shock response in alpha proteobacteria is unique in that a combination of two regulators isinvolved: a positive regulator, RpoH (32 homolog), found in the alpha, beta, and gamma proteobacteria,and a negative regulator, HrcA, widely distributed in eubacteria but not in the gamma proteobacteria. Toassess the differential roles of ... More
Cloning and subcellular localization of hamster and rat isopentenyl diphosphate dimethylallyl diphosphate isomerase. A PTS1 motif targets the enzyme to peroxisomes.
AuthorsPaton VG, Shackelford JE, Krisans SK
JournalJ Biol Chem
PubMed ID9228075
To date, isopentenyl diphosphate:dimethylallyl diphosphate isomerase (IPP isomerase; EC 5.3.3.2) is presumed to have a cytosolic localization. However, we have recently shown that in permeabilized cells lacking cytosolic components, mevalonate can be converted to cholesterol, implying that all of the enzymes required for the conversion of mevalonate to farnesyl diphosphate ... More
Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused.
Authors Kapust R B; Waugh D S;
JournalProtein Sci
PubMed ID10452611
Although it is usually possible to achieve a favorable yield of a recombinant protein in Escherichia coli, obtaining the protein in a soluble, biologically active form continues to be a major challenge. Sometimes this problem can be overcome by fusing an aggregation-prone polypeptide to a highly soluble partner. To study ... More