Nitrogenase metalloclusters: structures, organization, and synthesis

Dean, Dennis R.; Bolin, Jeffrey T.; Zheng, Limin

doi:10.1128/jb.175.21.6737-6744.1993

Cited by 213 publications

(171 citation statements)

References 60 publications

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“…Effect of the V102E Substitution on IscU Interactions with Hsc66 and Hsc20 -In addition to IscU, diazotrophpic organisms contain a second iron-sulfur template protein, NifU, that functions in the assembly of the nitrogenase protein (28,29). The N-terminal regions of NifU proteins display sequence homology to IscU proteins, but there are no known chaperones associated with iron-sulfur cluster assembly specific to the nitrogen fixation machinery (5,12).…”

Section: Stimulation Of Hsc66mentioning

confidence: 99%

Contributions of the LPPVK Motif of the Iron-Sulfur Template Protein IscU to Interactions with the Hsc66-Hsc20 Chaperone System

Hoff¹,

Cupp‐Vickery

Vickery

2003

Journal of Biological Chemistry

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Section: Stimulation Of Hsc66mentioning

confidence: 99%

Contributions of the LPPVK Motif of the Iron-Sulfur Template Protein IscU to Interactions with the Hsc66-Hsc20 Chaperone System

Hoff¹,

Cupp‐Vickery

Vickery

2003

Journal of Biological Chemistry

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“…In bacteria, the genes nifH, nifD and nifK, which encode the molybdenum-containing nitrogenase, are typically found together in a single operon and are physically adjacent to other nif genes as part of a larger nif regulon. Downstream of nifK, the nifE and nifN genes, which are essential for FeMo-cofactor assembly (Dean et al 1993), are found in a separate operon. In Archaea, genes homologous to the bacterial nif genes have been identified, and nitrogen fixation has been observed in several methanogenic species (Lobo and Zinder 1992, Young 1992, Bult et al 1996, Chien and Zinder 1996, Haselkorn and Buikema 1996, Kessler et al 1997, Smith et al 1997.…”

Section: Introductionmentioning

confidence: 99%

Functional organization of a single nif cluster in the mesophilic archaeon Methanosarcina mazei strain Gö1

Ehlers

Veit²,

Gottschalk³

et al. 2002

Archaea

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SummaryThe mesophilic methanogenic archaeon Methanosarcina mazei strain Gö1 is able to utilize molecular nitrogen (N 2 ) as its sole nitrogen source. We have identified and characterized a single nitrogen fixation (nif ) gene cluster in M. mazei Gö1 with an approximate length of 9 kbp. Sequence analysis revealed seven genes with sequence similarities to nifH, nifI 1 , nifI 2 , nifD, nifK, nifE and nif N, similar to other diazotrophic methanogens and certain bacteria such as Clostridium acetobutylicum, with the two glnB-like genes (nifI 1 and nifI 2 ) located between nifH and nifD. Phylogenetic analysis of deduced amino acid sequences for the nitrogenase structural genes of M. mazei Gö1 showed that they are most closely related to Methanosarcina barkeri nif 2 genes, and also closely resemble those for the corresponding nif products of the grampositive bacterium C. acetobutylicum. Northern blot analysis and reverse transcription PCR analysis demonstrated that the M. mazei nif genes constitute an operon transcribed only under nitrogen starvation as a single 8 kb transcript. Sequence analysis revealed a palindromic sequence at the transcriptional start site in front of the M. mazei nifH gene, which may have a function in transcriptional regulation of the nif operon.

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“…Data from in vitro biochemical and spectroscopic studies 27,44,45,49 coupled with results from in vivo experiments 33,39,40,50 strongly suggested that IscU is a biological scaffold for Fe-S cluster assembly. Further support for such a role came from far-UV CD 26 and NMR 48 studies, which showed essentially identical secondary structural content and similar tertiary structural and dynamic properties for apo and holo T. maritima IscU, i.e., unlike other low molecular weight metalloproteins, IscU retains its tertiary structure in the apo state that is preformed for Fe-S cluster coordination.…”

Section: Cast Of Characters In Iron-sulfur Cluster Biosynthesismentioning

confidence: 99%

“…Initial evidence for the function of IscU (prokaryotic) [or ISU (eukaryotic)] was based on genetic and cell biology studies that implicated IscU in Fe-S cluster biosynthesis. 39,40 However, these studies could not differentiate between IscU functioning as an iron or an iron-sulfur cluster delivery protein. Given our long-standing interest in Fe-S biochemistry and mechanisms of cluster assembly and disassembly, [41][42][43] we initiated a program to compare and contrast the properties of IscU from a variety of sources, including human (Hs ISU), yeast (Schizosaccharomyces pombe, Sp ISU), and a hyperthermophilic bacterium (Thermotoga maritima, Tm IscU).…”

Section: Cast Of Characters In Iron-sulfur Cluster Biosynthesismentioning

confidence: 99%

Iron Sulfur Cluster Biosynthesis

Cowan

2009

ACS Symposium Series

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Iron-sulfur clusters are among the most complex metal-containing prosthetic centers in biology. Most if not all of the proteins involved in the biosynthesis of "simple" Fe-S clusters have been identified. The structural and functional chemistry of these proteins has been the subject of intense research efforts, and many of the key details are now understood in structural and mechanistic detail. The fact that Fe-S cluster-binding proteins can be reconstituted in vitro with no accessory proteins provides an important indicator of the intracellular roles for many proteins on the Fe-S cluster assembly pathway. Indeed, such proteins are more correctly viewed as carrier proteins, rather than as catalysts for the reaction, that both avoid the toxicity associated with free iron and sulfide and allow delivery at lower intracellular concentrations of these species. The IscU (or ISU) family of proteins serves a key role as scaffolding proteins on which [2Fe-2S] building blocks are assembled prior to transfer to final apo target proteins. IscU in particular exhibits highly unusual conformational flexibility that appears critical to its function.

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Nitrogenase metalloclusters: structures, organization, and synthesis

Cited by 213 publications

References 60 publications

Contributions of the LPPVK Motif of the Iron-Sulfur Template Protein IscU to Interactions with the Hsc66-Hsc20 Chaperone System

Contributions of the LPPVK Motif of the Iron-Sulfur Template Protein IscU to Interactions with the Hsc66-Hsc20 Chaperone System

Functional organization of a single nif cluster in the mesophilic archaeon Methanosarcina mazei strain Gö1

Iron Sulfur Cluster Biosynthesis

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